{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"http://dx.doi.org/10.1002/lipd.12285","label":"url"},{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2010623","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=371661","label":"url"}],"paper_title":{"en":"Massspectrometric analysis of sphingomyelin with N-alfa-hydroxy fatty acyl residue in mouse tissues","ja":"Massspectrometric analysis of sphingomyelin with N-alfa-hydroxy fatty acyl residue in mouse tissues"},"authors":{"en":[{"name":"Ali Hanif"},{"name":"Yamashita Ryouhei"},{"name":"Morishige Jun-ichi"},{"name":"Morito Katsuya"},{"name":"Kakiuchi Naoya"},{"name":"Hayashi Junji"},{"name":"Aihara Mutsumi"},{"name":"Kawakami Ryushi"},{"name":"Tsuchiya Koichiro"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"MD HANIF ALI"},{"name":"山下 量平"},{"name":"盛重 純一"},{"name":"森戸 克弥"},{"name":"柿内 直哉"},{"name":"林 順司"},{"name":"粟飯原 睦美"},{"name":"川上 竜巳"},{"name":"土屋 浩一郎"},{"name":"田中 保"}]},"publication_date":"2021-09","publication_name":{"en":"Lipids","ja":"Lipids"},"volume":"56","number":"2","starting_page":"181","ending_page":"188","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1002/lipd.12285"],"issn":["1558-9307"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/32585250","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85087143410","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=370498","label":"url"}],"paper_title":{"en":"Distinct contributions of two choline-producing enzymatic activities to lysophosphatidic acid production in human amniotic fluid from pregnant women in the second trimester and after parturition","ja":"Distinct contributions of two choline-producing enzymatic activities to lysophosphatidic acid production in human amniotic fluid from pregnant women in the second trimester and after parturition"},"authors":{"en":[{"name":"Fukui Midori"},{"name":"Tsutsumi Toshihiko"},{"name":"Yamamoto-Mikami Aimi"},{"name":"Morito Katsuya"},{"name":"Takahashi Naoko"},{"name":"Tanaka Tamotsu"},{"name":"Iwasa Tekeshi"},{"name":"Kuwahara Akira"},{"name":"Irahara Minoru"},{"name":"Tokumura Akira"}],"ja":[{"name":"福井 翠"},{"name":"堤 俊彦"},{"name":"山本 藍美"},{"name":"森戸 克弥"},{"name":"髙橋 尚子"},{"name":"田中 保"},{"name":"Iwasa Tekeshi"},{"name":"桑原 章"},{"name":"苛原 稔"},{"name":"德村 彰"}]},"publication_date":"2020-10","publication_name":{"en":"Prostaglandins & Other Lipid Mediators","ja":"Prostaglandins & Other Lipid Mediators"},"volume":"150","starting_page":"106471","ending_page":"106471","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.prostaglandins.2020.106471"],"issn":["1098-8823"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=370543","label":"url"}],"paper_title":{"en":"Identification of human glycerophosphodiesterase 3 as an ectophospholipase C that converts the G protein-coupled receptor 55 agonist lysophosphatidylinositol to bioactive monoacylglycerols in cultured mammalian cells.","ja":"Identification of human glycerophosphodiesterase 3 as an ectophospholipase C that converts the G protein-coupled receptor 55 agonist lysophosphatidylinositol to bioactive monoacylglycerols in cultured mammalian cells."},"authors":{"en":[{"name":"Tsutsumi Toshihiko"},{"name":"Matsuda Risa"},{"name":"Morito Katsuya"},{"name":"Kawabata Kohei"},{"name":"Yokota Miho"},{"name":"Nikawadori Miki"},{"name":"Inoue-Fujiwara Manami"},{"name":"Kawashima Satoshi"},{"name":"Hidaka Mayumi"},{"name":"Yamamoto Takenori"},{"name":"Yamazaki Naoshi"},{"name":"Tanaka Tamotsu"},{"name":"Shinohara Yasuo"},{"name":"Nishi Hiroyuki"},{"name":"Tokumura Akira"}],"ja":[{"name":"堤 敏彦"},{"name":"松田 璃沙"},{"name":"森戸 克弥"},{"name":"Kawabata Kohei"},{"name":"横田 美帆"},{"name":"荷川取 史妃"},{"name":"Inoue-Fujiwara Manami"},{"name":"Kawashima Satoshi"},{"name":"Hidaka Mayumi"},{"name":"山本 武範"},{"name":"山﨑 尚志"},{"name":"田中 保"},{"name":"篠原 康雄"},{"name":"Nishi Hiroyuki"},{"name":"德村 彰"}]},"publication_date":"2020-09","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids","ja":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"},"volume":"1865","number":"9","starting_page":"158761","ending_page":"158761","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbalip.2020.158761"],"issn":["1388-1981"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2008132","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/32615533","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=370497","label":"url"}],"paper_title":{"en":"Isolation of glycosylinositol phosphoceramide and phytoceramide 1-phosphate in plants and their chemical stabilities.","ja":"Isolation of glycosylinositol phosphoceramide and phytoceramide 1-phosphate in plants and their chemical stabilities."},"authors":{"en":[{"name":"Hasi Yesmin Rumana"},{"name":"Majima Dai"},{"name":"Morito Katsuya"},{"name":"Ali Hanif"},{"name":"Kogure Kentaro"},{"name":"Nanjundan Meera"},{"name":"Hayashi Junji"},{"name":"Kawakami Ryushi"},{"name":"Kanemaru Kaori"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Rumana Hasi Yesmin"},{"name":"真島 大"},{"name":"森戸 克弥"},{"name":"MD HANIF ALI"},{"name":"小暮 健太朗"},{"name":"ミエラ ナンジュンダン"},{"name":"林 順司"},{"name":"川上 竜巳"},{"name":"金丸 芳"},{"name":"田中 保"}]},"description":{"en":"Glycosylinositol phosphoceramide (GIPC) is a sphingophospholipid in plants. Recently, we identified that GIPC is hydrolyzed to phytoceramide 1-phosphate (PC1P) by an uncharacterized phospholipase D activity following homogenization of certain plant tissues. We now developed methods for isolation of GIPC and PC1P from plant tissues and characterized their chemical stabilities. Hydrophilic solvents, namely a lower layer of a mixed solvent system consisting of isopropanol/hexane/water (55:20:25, v/v/v) was efficient solvent for extraction and eluent in column chromatography. GIPC was isolated by Sephadex column chromatography followed by TLC. A conventional method, such as the Bligh and Dyer method, was applicable for PC1P extraction. Specifically, PC1P was isolated by TLC following mild alkali treatment of lipid extracts of plants. The yields of GIPC and PC1P in our methods were both around 50-70%. We found that PC1P is tolerant against heat (up to 125 °C), strong acid (up to 10 M HCl), and mild alkali (0.1 M KOH). In contrast, significant degradation of GIPC occurred at 100 °C and 1.0 M HCl treatment, suggesting the instability of the inositol glycan moiety in these conditions. These data will be useful for further biochemical and nutritional studies on these sphingolipids.","ja":"Glycosylinositol phosphoceramide (GIPC) is a sphingophospholipid in plants. Recently, we identified that GIPC is hydrolyzed to phytoceramide 1-phosphate (PC1P) by an uncharacterized phospholipase D activity following homogenization of certain plant tissues. We now developed methods for isolation of GIPC and PC1P from plant tissues and characterized their chemical stabilities. Hydrophilic solvents, namely a lower layer of a mixed solvent system consisting of isopropanol/hexane/water (55:20:25, v/v/v) was efficient solvent for extraction and eluent in column chromatography. GIPC was isolated by Sephadex column chromatography followed by TLC. A conventional method, such as the Bligh and Dyer method, was applicable for PC1P extraction. Specifically, PC1P was isolated by TLC following mild alkali treatment of lipid extracts of plants. The yields of GIPC and PC1P in our methods were both around 50-70%. We found that PC1P is tolerant against heat (up to 125 °C), strong acid (up to 10 M HCl), and mild alkali (0.1 M KOH). In contrast, significant degradation of GIPC occurred at 100 °C and 1.0 M HCl treatment, suggesting the instability of the inositol glycan moiety in these conditions. These data will be useful for further biochemical and nutritional studies on these sphingolipids."},"publication_date":"2020-06-12","publication_name":{"en":"Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences","ja":"Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences"},"volume":"1152","starting_page":"122213","ending_page":"122213","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.jchromb.2020.122213"],"issn":["1873-376X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.scopus.com/pages/publications/85071868836","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=361538","label":"url"}],"paper_title":{"en":"Intracellular Ca2+-dependent formation of N-acyl-phosphatidylethanolamines by human cytosolic phospholipase A2ϵ.","ja":"Intracellular Ca2+-dependent formation of N-acyl-phosphatidylethanolamines by human cytosolic phospholipase A2ϵ."},"authors":{"en":[{"name":"Mustafiz Binte Sultana Smriti"},{"name":"Uyama Toru"},{"name":"Morito Katsuya"},{"name":"Takahashi Naoko"},{"name":"Kawai Katsuhisa"},{"name":"Hussain Zahir"},{"name":"Tsuboi Kazuhito"},{"name":"Araki Nobukazu"},{"name":"Yamamoto Kei"},{"name":"Tanaka Tamotsu"},{"name":"Ueda Natsuo"}],"ja":[{"name":"Mustafiz Binte Sultana Smriti"},{"name":"Uyama Toru"},{"name":"森戸 克弥"},{"name":"Takahashi Naoko"},{"name":"Kawai Katsuhisa"},{"name":"Hussain Zahir"},{"name":"Tsuboi Kazuhito"},{"name":"Araki Nobukazu"},{"name":"山本 圭"},{"name":"田中 保"},{"name":"Ueda Natsuo"}]},"publication_date":"2019-12","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids","ja":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"},"volume":"1864","number":"12","starting_page":"158515","ending_page":"158515","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbalip.2019.158515"],"issn":["1388-1981"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2006703","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/31351225","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=359915","label":"url"}],"paper_title":{"en":"Gut microbial metabolites of linoleic acid are metabolized by accelerated peroxisomal β-oxidation in mammalian cells","ja":"Gut microbial metabolites of linoleic acid are metabolized by accelerated peroxisomal β-oxidation in mammalian cells"},"authors":{"en":[{"name":"Morito Katsuya"},{"name":"Shimizu Ryota"},{"name":"Kitamura Nahoko"},{"name":"Park Si-Bum"},{"name":"Kishino Shigenobu"},{"name":"Ogawa Jun"},{"name":"Fukuta Tatsuya"},{"name":"Kogure Kentaro"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"森戸 克弥"},{"name":"清水 良多"},{"name":"Kitamura Nahoko"},{"name":"Park Si-Bum"},{"name":"Kishino Shigenobu"},{"name":"Ogawa Jun"},{"name":"福田 達也"},{"name":"小暮 健太朗"},{"name":"田中 保"}]},"description":{"en":"Microorganisms in animal gut produce unusual fatty acids from the ingested diet. Two types of hydroxy fatty acids (HFAs), 10-hydroxy-cis-12-octadecenoic acid (HYA) and 10-hydroxy-octadecanoic acid (HYB), are linoleic acid (LA) metabolites produced by Lactobacillus plantarum. In this study, we investigated the metabolism of these HFAs in mammalian cells. When Chinese hamster ovary (CHO) cells were cultured with HYA, approximately 50% of the supplemented HYA disappeared from the dish within 24 h. On the other hand, the amount of HYA that disappeared from the dish of peroxisome (PEX)-deficient CHO cells was lower than 20%. Significant amounts of C2- and C4-chain-shortened metabolites of HYA were detected in culture medium of HYA-supplemented CHO cells, but not in medium of PEX-deficient cells. These results suggested that peroxisomal β-oxidation is involved in the disappearance of HYA. The PEX-dependent disappearance was observed in the experiment with HYB, but not with LA. We also found that HYA treatment up-regulates peroxisomal β-oxidation activity of human gastric MKN74 cells and intestinal Caco-2 cells. These results indicate a possibility that HFAs produced from gut bacteria affect lipid metabolism of host via modulation of peroxisomal β-oxidation activity.","ja":"Microorganisms in animal gut produce unusual fatty acids from the ingested diet. Two types of hydroxy fatty acids (HFAs), 10-hydroxy-cis-12-octadecenoic acid (HYA) and 10-hydroxy-octadecanoic acid (HYB), are linoleic acid (LA) metabolites produced by Lactobacillus plantarum. In this study, we investigated the metabolism of these HFAs in mammalian cells. When Chinese hamster ovary (CHO) cells were cultured with HYA, approximately 50% of the supplemented HYA disappeared from the dish within 24 h. On the other hand, the amount of HYA that disappeared from the dish of peroxisome (PEX)-deficient CHO cells was lower than 20%. Significant amounts of C2- and C4-chain-shortened metabolites of HYA were detected in culture medium of HYA-supplemented CHO cells, but not in medium of PEX-deficient cells. These results suggested that peroxisomal β-oxidation is involved in the disappearance of HYA. The PEX-dependent disappearance was observed in the experiment with HYB, but not with LA. We also found that HYA treatment up-regulates peroxisomal β-oxidation activity of human gastric MKN74 cells and intestinal Caco-2 cells. These results indicate a possibility that HFAs produced from gut bacteria affect lipid metabolism of host via modulation of peroxisomal β-oxidation activity."},"publication_date":"2019-11","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids","ja":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"},"volume":"1864","number":"11","starting_page":"1619","ending_page":"1628","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbalip.2019.07.010"],"issn":["1879-2618"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2006706","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/31504617","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85073764089","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=363542","label":"url"}],"paper_title":{"en":"Glycosylinositol phosphoceramide-specific phospholipase D activity catalyzes transphosphatidylation","ja":"Glycosylinositol phosphoceramide-specific phospholipase D activity catalyzes transphosphatidylation"},"authors":{"en":[{"name":"Rumana Yesmin Hasi"},{"name":"Miyagi Makoto"},{"name":"Morito Katsuya"},{"name":"Ishikawa Toshiki"},{"name":"Kawai-Yamada Maki"},{"name":"Imai Hiroyuki"},{"name":"Fukuta Tatsuya"},{"name":"Kogure Kentaro"},{"name":"Kanemaru Kaori"},{"name":"Hayashi Junji"},{"name":"Kawakami Ryushi"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Rumana Hasi Yesmin"},{"name":"宮城 諒"},{"name":"森戸 克弥"},{"name":"Ishikawa Toshiki"},{"name":"Kawai-Yamada Maki"},{"name":"Imai Hiroyuki"},{"name":"福田 達也"},{"name":"小暮 健太朗"},{"name":"金丸 芳"},{"name":"林 順司"},{"name":"川上 竜巳"},{"name":"田中 保"}]},"description":{"en":"Glycosylinositol phosphoceramide (GIPC) is the most abundant sphingolipid in plants and fungi. Recently, we detected GIPC-specific phospholipase D (GIPC-PLD) activity in plants. Here, we found that GIPC-PLD activity in young cabbage leaves catalyzes transphosphatidylation. The available alcohol for this reaction is a primary alcohol with a chain length below C4. Neither secondary alcohol, tertiary alcohol, choline, serine nor glycerol serves as an acceptor for transphosphatidylation of GIPC-PLD. We also found that cabbage GIPC-PLD prefers GIPC containing two sugars. Neither inositol phosphoceramide, mannosylinositol phosphoceramide nor GIPC with three sugar chains served as substrate. GIPC-PLD will become a useful catalyst for modification of polar head group of sphingophospholipid.","ja":"Glycosylinositol phosphoceramide (GIPC) is the most abundant sphingolipid in plants and fungi. Recently, we detected GIPC-specific phospholipase D (GIPC-PLD) activity in plants. Here, we found that GIPC-PLD activity in young cabbage leaves catalyzes transphosphatidylation. The available alcohol for this reaction is a primary alcohol with a chain length below C4. Neither secondary alcohol, tertiary alcohol, choline, serine nor glycerol serves as an acceptor for transphosphatidylation of GIPC-PLD. We also found that cabbage GIPC-PLD prefers GIPC containing two sugars. Neither inositol phosphoceramide, mannosylinositol phosphoceramide nor GIPC with three sugar chains served as substrate. GIPC-PLD will become a useful catalyst for modification of polar head group of sphingophospholipid."},"publication_date":"2019-08-26","publication_name":{"en":"The Journal of Biochemistry","ja":"The Journal of Biochemistry"},"volume":"166","number":"5","starting_page":"441","ending_page":"448","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1093/jb/mvz056"],"issn":["1756-2651"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/30368958","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85055676743","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=358659","label":"url"}],"paper_title":{"en":"Addition of high load of lysophosphatidic acid to standard and high-fat chows causes no significant changes of its circulating and peripheral tissue levels but affects body weight and visceral fat mass of mice.","ja":"Addition of high load of lysophosphatidic acid to standard and high-fat chows causes no significant changes of its circulating and peripheral tissue levels but affects body weight and visceral fat mass of mice."},"authors":{"en":[{"name":"Inoue Manami"},{"name":"Okamoto Yoko"},{"name":"Atsumi Yuta"},{"name":"Shiojiri Masatoshi"},{"name":"Hidaka Mayumi"},{"name":"Tanaka Tamotsu"},{"name":"Tsutsumi Toshihiko"},{"name":"Shirasaka Naoki"},{"name":"Tokumura Akira"}],"ja":[{"name":"Inoue Manami"},{"name":"Okamoto Yoko"},{"name":"Atsumi Yuta"},{"name":"Shiojiri Masatoshi"},{"name":"Hidaka Mayumi"},{"name":"田中 保"},{"name":"Tsutsumi Toshihiko"},{"name":"Shirasaka Naoki"},{"name":"Tokumura Akira"}]},"description":{"en":"Oral administration of lysophosphatidic acid (LPA), a critical intercellular lipid mediator, exerts wound healing and antiulcer effects on gastrointestinal system. To evaluate effects of food-derived LPA on body homeostasis, we measured LPA levels by liquid chromatography-tandem mass spectrometry in chows, feces, plasma, liver, and visceral fat of mice fed a normal or high-fat chow supplemented with or without LPA-rich soybean phospholipids for 30 days. Reductions in daily body weight gains and visceral fat mass were mainly related to lower chow intake by mice fed the LPA-rich high-fat chow, whereas reduced body weight gains and fat mass were mainly related to decreased intestinal triacylglycerol absorption in mice fed LPA-rich chow. Our results showed no significant increase in plasma, liver, or adipose LPA levels, even if a quite high LPA concentration (2.0%) in chows was ingested daily, suggesting limited effects of food-derived LPA on the lumen side of the digestive tract. © 2018 BioFactors, 44(6):548-557, 2018.","ja":"Oral administration of lysophosphatidic acid (LPA), a critical intercellular lipid mediator, exerts wound healing and antiulcer effects on gastrointestinal system. To evaluate effects of food-derived LPA on body homeostasis, we measured LPA levels by liquid chromatography-tandem mass spectrometry in chows, feces, plasma, liver, and visceral fat of mice fed a normal or high-fat chow supplemented with or without LPA-rich soybean phospholipids for 30 days. Reductions in daily body weight gains and visceral fat mass were mainly related to lower chow intake by mice fed the LPA-rich high-fat chow, whereas reduced body weight gains and fat mass were mainly related to decreased intestinal triacylglycerol absorption in mice fed LPA-rich chow. Our results showed no significant increase in plasma, liver, or adipose LPA levels, even if a quite high LPA concentration (2.0%) in chows was ingested daily, suggesting limited effects of food-derived LPA on the lumen side of the digestive tract. © 2018 BioFactors, 44(6):548-557, 2018."},"publication_date":"2018-10-16","publication_name":{"en":"BioFactors","ja":"BioFactors"},"volume":"44","number":"6","starting_page":"548","ending_page":"557","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1002/biof.1451"],"issn":["1872-8081"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2005189","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/29462674","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85042401633","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=339054","label":"url"}],"paper_title":{"en":"Lysophosphatidic acid in medicinal herbs enhances prostaglandin E2 and protects against indomethacin-induced gastric cell damage in vivo and in vitro","ja":"Lysophosphatidic acid in medicinal herbs enhances prostaglandin E2 and protects against indomethacin-induced gastric cell damage in vivo and in vitro"},"authors":{"en":[{"name":"Afroz Sheuli"},{"name":"Yagi Ayano"},{"name":"Fujikawa Kouki"},{"name":"Rahman Motiur M."},{"name":"Morito Katsuya"},{"name":"Fukuta Tatsuya"},{"name":"Watanabe Shiro"},{"name":"Toida Kazunori"},{"name":"Kiyokage Emi"},{"name":"Shimizu Taro"},{"name":"Ishida Tatsuhiro"},{"name":"Kogure Kentaro"},{"name":"Tokumura Akira"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"SHEULI AFROZ"},{"name":"屋宜 亜耶乃"},{"name":"藤川 昂樹"},{"name":"Md. Motiur Rahman"},{"name":"森戸 克弥"},{"name":"福田 達也"},{"name":"Watanabe Shiro"},{"name":"Toida Kazunori"},{"name":"Kiyokage Emi"},{"name":"清水 太郎"},{"name":"石田 竜弘"},{"name":"小暮 健太朗"},{"name":"德村 彰"},{"name":"田中 保"}]},"description":{"en":"Lysophosphatidic acid (LPA) is a bioactive phospholipid that induces diverse biological responses. Recently, we found that LPA ameliorates NSAIDs-induced gastric ulcer in mice. Here, we quantified LPA in 21 medicinal herbs used for treatment of gastrointestinal (GI) disorders. We found that half of them contained LPA at relatively high levels (40-240 μg/g) compared to soybean seed powder (4.6 μg/g), which we previously identified as an LPA-rich food. The LPA in peony (Paeonia lactiflora) root powder is highly concentrated in the lipid fraction that ameliorates indomethacin-induced gastric ulcer in mice. Synthetic 18:1 LPA, peony root LPA and peony root lipid enhanced prostaglandin E production in a gastric cancer cell line, MKN74 cells that express LPA abundantly. These materials also prevented indomethacin-induced cell death and stimulated the proliferation of MKN74 cells. We found that LPA was present in stomach fluids at 2.4 μM, which is an effective LPA concentration for inducing a cellular response in vitro. These results indicated that LPA is one of the active components of medicinal herbs for the treatment of GI disorder and that orally administered LPA-rich herbs may augment the protective actions of endogenous LPA on gastric mucosa.","ja":"Lysophosphatidic acid (LPA) is a bioactive phospholipid that induces diverse biological responses. Recently, we found that LPA ameliorates NSAIDs-induced gastric ulcer in mice. Here, we quantified LPA in 21 medicinal herbs used for treatment of gastrointestinal (GI) disorders. We found that half of them contained LPA at relatively high levels (40-240 μg/g) compared to soybean seed powder (4.6 μg/g), which we previously identified as an LPA-rich food. The LPA in peony (Paeonia lactiflora) root powder is highly concentrated in the lipid fraction that ameliorates indomethacin-induced gastric ulcer in mice. Synthetic 18:1 LPA, peony root LPA and peony root lipid enhanced prostaglandin E production in a gastric cancer cell line, MKN74 cells that express LPA abundantly. These materials also prevented indomethacin-induced cell death and stimulated the proliferation of MKN74 cells. We found that LPA was present in stomach fluids at 2.4 μM, which is an effective LPA concentration for inducing a cellular response in vitro. These results indicated that LPA is one of the active components of medicinal herbs for the treatment of GI disorder and that orally administered LPA-rich herbs may augment the protective actions of endogenous LPA on gastric mucosa."},"publication_date":"2018-01-25","publication_name":{"en":"Prostaglandins & Other Lipid Mediators","ja":"Prostaglandins & Other Lipid Mediators"},"volume":"135","starting_page":"36","ending_page":"44","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.prostaglandins.2018.01.003"],"issn":["1098-8823"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28992041","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85029655027","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=344832","label":"url"}],"paper_title":{"en":"Peripheral tissue levels and molecular species compositions of N-acyl-phosphatidylethanolamine and its metabolites in mice lacking N-acyl-phosphatidylethanolamine-specific phospholipase D.","ja":"Peripheral tissue levels and molecular species compositions of N-acyl-phosphatidylethanolamine and its metabolites in mice lacking N-acyl-phosphatidylethanolamine-specific phospholipase D."},"authors":{"en":[{"name":"Inoue Manami"},{"name":"Tsuboi Kazuhito"},{"name":"Okamoto Yoko"},{"name":"Hidaka Mayumi"},{"name":"Uyama Toru"},{"name":"Tsutsumi Toshihiko"},{"name":"Tanaka Tamotsu"},{"name":"Ueda Natsuo"},{"name":"Tokumura Akira"}],"ja":[{"name":"Inoue Manami"},{"name":"Tsuboi Kazuhito"},{"name":"Okamoto Yoko"},{"name":"Hidaka Mayumi"},{"name":"Uyama Toru"},{"name":"Tsutsumi Toshihiko"},{"name":"田中 保"},{"name":"Ueda Natsuo"},{"name":"德村 彰"}]},"description":{"en":"N-acylethanolamines (NAEs), a class of lipid mediators, are produced from N-acyl-phosphatidylethanolamine (NAPE) by several pathways, including the direct release by NAPE-specific phospholipase D (NAPE-PLD) or the multistep pathway via sn-glycero-3-phospho-N-acylethanolamine (Gp-NAE). Using liquid chromatography-tandem mass spectrometry, we compared peripheral tissue levels of NAPE, Gp-NAE and NAE in NAPE-PLD-deficient (NAPE-PLD-/-) and wild type (WT) mice. NAPE-PLD was suggested to play a major role in the NAPE degradation in heart, kidney, and liver, but not in jejunum, because the NAPE levels except jejunum were significantly higher in NAPE-PLD-/- mice than in WT mice. The deletion of NAPE-PLD failed to alter the NAE levels of these tissues, suggesting its limited role in the NAE production. The enzyme assays with tissue homogenates confirmed the presence of NAPE-PLD-independent pathways in these peripheral tissues. Gp-NAE species having an acyl moiety with 22 carbons and 6 double bonds was enriched in these peripheral tissues. As for sn-2 acyl species of NAPE, 18:2-acyl-containing NAPE species were predominant over 18:1-containing species in heart, liver, and jejunum. Our results show that both molecular species composition of NAPE, NAE and Gp-NAE and their dependencies on Napepld are different among the peripheral tissues, suggesting that each tissue has distinct metabolic pathways and these NAE-containing lipids play tissue-specific roles.","ja":"N-acylethanolamines (NAEs), a class of lipid mediators, are produced from N-acyl-phosphatidylethanolamine (NAPE) by several pathways, including the direct release by NAPE-specific phospholipase D (NAPE-PLD) or the multistep pathway via sn-glycero-3-phospho-N-acylethanolamine (Gp-NAE). Using liquid chromatography-tandem mass spectrometry, we compared peripheral tissue levels of NAPE, Gp-NAE and NAE in NAPE-PLD-deficient (NAPE-PLD-/-) and wild type (WT) mice. NAPE-PLD was suggested to play a major role in the NAPE degradation in heart, kidney, and liver, but not in jejunum, because the NAPE levels except jejunum were significantly higher in NAPE-PLD-/- mice than in WT mice. The deletion of NAPE-PLD failed to alter the NAE levels of these tissues, suggesting its limited role in the NAE production. The enzyme assays with tissue homogenates confirmed the presence of NAPE-PLD-independent pathways in these peripheral tissues. Gp-NAE species having an acyl moiety with 22 carbons and 6 double bonds was enriched in these peripheral tissues. As for sn-2 acyl species of NAPE, 18:2-acyl-containing NAPE species were predominant over 18:1-containing species in heart, liver, and jejunum. Our results show that both molecular species composition of NAPE, NAE and Gp-NAE and their dependencies on Napepld are different among the peripheral tissues, suggesting that each tissue has distinct metabolic pathways and these NAE-containing lipids play tissue-specific roles."},"publication_date":"2017-12-01","publication_name":{"en":"The Journal of Biochemistry","ja":"The Journal of Biochemistry"},"volume":"162","number":"6","starting_page":"449","ending_page":"458","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1093/jb/mvx054"],"issn":["1756-2651"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2010624","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28175321","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1522262180608136704/","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85015919191","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=338861","label":"url"}],"paper_title":{"en":"Distribution of glycosylinositol phosphoceramide-specific phospholipase D activity in plants","ja":"Distribution of glycosylinositol phosphoceramide-specific phospholipase D activity in plants"},"authors":{"en":[{"name":"Takashi Kida"},{"name":"Aoi Itoh"},{"name":"Akari Kimura"},{"name":"Hisatsugu Matsuoka"},{"name":"Hiroyuki Imai"},{"name":"Kogure Kentaro"},{"name":"Tokumura Akira"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"喜田 孝史"},{"name":"Aoi Itoh"},{"name":"Akari Kimura"},{"name":"Hisatsugu Matsuoka"},{"name":"Hiroyuki Imai"},{"name":"小暮 健太朗"},{"name":"德村 彰"},{"name":"田中 保"}]},"description":{"en":"Previously, we detected an unknown sphingophospholipid in cabbage leaves and identified it as phytoceramide-1-phosphate (PC1P). We also found an enzyme activity that produces PC1P by glycosylinositol phosphoceramide (GIPC)-specific hydrolysis in cabbage leaves. To characterize the GIPC-specific phospholipase D (GIPC-PLD) activity, we investigated distributions of GIPC-PLD activity in 25 tissues of 10 plants. In most plants, the GIPC-PLD activity was the highest in roots. Young leaves of cabbage and Welsh onion had higher activities than corresponding aged outer leaves. The GIPC-PLD activities in leaves, stems and roots of mung bean were higher in the sprouting stage than in more mature stages. We also examined the distribution of substrate GIPC and product PC1P and found that GIPC was ubiquitously distributed at 50-280 nmol/g (wet wt) in tissues of plants, whereas PC1P was detectable (3-60 nmol/g wet wt.) only in tissues showing considerable GIPC-PLD activity. These results suggest a possibility that GIPC-PLD activity is involved in plant growth.","ja":"Previously, we detected an unknown sphingophospholipid in cabbage leaves and identified it as phytoceramide-1-phosphate (PC1P). We also found an enzyme activity that produces PC1P by glycosylinositol phosphoceramide (GIPC)-specific hydrolysis in cabbage leaves. To characterize the GIPC-specific phospholipase D (GIPC-PLD) activity, we investigated distributions of GIPC-PLD activity in 25 tissues of 10 plants. In most plants, the GIPC-PLD activity was the highest in roots. Young leaves of cabbage and Welsh onion had higher activities than corresponding aged outer leaves. The GIPC-PLD activities in leaves, stems and roots of mung bean were higher in the sprouting stage than in more mature stages. We also examined the distribution of substrate GIPC and product PC1P and found that GIPC was ubiquitously distributed at 50-280 nmol/g (wet wt) in tissues of plants, whereas PC1P was detectable (3-60 nmol/g wet wt.) only in tissues showing considerable GIPC-PLD activity. These results suggest a possibility that GIPC-PLD activity is involved in plant growth."},"publication_date":"2017-02-01","publication_name":{"en":"The Journal of Biochemistry","ja":"The Journal of Biochemistry"},"volume":"161","number":"2","starting_page":"187","ending_page":"195","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1093/jb/mvw060"],"issn":["1756-2651"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/27561232","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=327660","label":"url"}],"paper_title":{"en":"Concentrated phosphatidic acid in cereal brans as potential protective agents against indomethacin-induced stomach ulcer.","ja":"Concentrated phosphatidic acid in cereal brans as potential protective agents against indomethacin-induced stomach ulcer."},"authors":{"en":[{"name":"Afroz S"},{"name":"Ikoma Teru"},{"name":"Yagi Ayano"},{"name":"Kogure Kentaro"},{"name":"Tokumura Akira"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Afroz S"},{"name":"生駒 照"},{"name":"屋宜 亜耶乃"},{"name":"小暮 健太朗"},{"name":"德村 彰"},{"name":"田中 保"}]},"description":{"en":"One of complications associated with long-term use of nonsteroidal anti-inflammatory drugs (NSAIDs) is peptic ulcer. Recently, we found that orally administered phosphatidic acid (PA) ameliorated aspirin-induced stomach lesions in mice. In this study, we identified PA-rich food sources and examined the effects of the food materials on indomethacin-induced stomach ulcer. Among examined, buckwheat (Fagopyrum esculentum) bran contained the highest level of PA (188 mg/100 g). PA was the richest phospholipid (25%) in the lipid fraction of the buckwheat bran. Administration of the lipid extracts of buckwheat bran significantly ameliorated indomethacin-induced stomach lesions in mice. In contrast, wheat (Triticum durum) bran lipids (PA, 4%) and soybean (Glycine max) lipids (PA, 3%) were not associated with ameliorative effects. These results indicated that PA-rich lipids can be used as an effective supplement for prevention of NSAID-induced stomach ulcer.","ja":"One of complications associated with long-term use of nonsteroidal anti-inflammatory drugs (NSAIDs) is peptic ulcer. Recently, we found that orally administered phosphatidic acid (PA) ameliorated aspirin-induced stomach lesions in mice. In this study, we identified PA-rich food sources and examined the effects of the food materials on indomethacin-induced stomach ulcer. Among examined, buckwheat (Fagopyrum esculentum) bran contained the highest level of PA (188 mg/100 g). PA was the richest phospholipid (25%) in the lipid fraction of the buckwheat bran. Administration of the lipid extracts of buckwheat bran significantly ameliorated indomethacin-induced stomach lesions in mice. In contrast, wheat (Triticum durum) bran lipids (PA, 4%) and soybean (Glycine max) lipids (PA, 3%) were not associated with ameliorative effects. These results indicated that PA-rich lipids can be used as an effective supplement for prevention of NSAID-induced stomach ulcer."},"publication_date":"2016-12","publication_name":{"en":"Journal of Agricultural and Food Chemistry","ja":"Journal of Agricultural and Food Chemistry"},"volume":"64","number":"37","starting_page":"6950","ending_page":"6957","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1021/acs.jafc.6b02884"],"issn":["1520-5118"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/27637550","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84988489470","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=322570","label":"url"}],"paper_title":{"en":"Calcium-dependent generation of N-acylethanolamines and lysophosphatidic acids by glycerophosphodiesterase GDE7.","ja":"Calcium-dependent generation of N-acylethanolamines and lysophosphatidic acids by glycerophosphodiesterase GDE7."},"authors":{"en":[{"name":"Rahman Sonia Ara Iffat"},{"name":"Tsuboi Kazuhito"},{"name":"Hussain Zahir"},{"name":"Yamashita Ryouhei"},{"name":"Okamoto Yoko"},{"name":"Uyama Toru"},{"name":"Yamazaki Naoshi"},{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"},{"name":"Ueda Natsuo"}],"ja":[{"name":"Rahman Sonia Ara Iffat"},{"name":"Tsuboi Kazuhito"},{"name":"Hussain Zahir"},{"name":"Yamashita Ryouhei"},{"name":"Okamoto Yoko"},{"name":"Uyama Toru"},{"name":"山﨑 尚志"},{"name":"田中 保"},{"name":"德村 彰"},{"name":"Ueda Natsuo"}]},"publication_date":"2016-12","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids","ja":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"},"volume":"1861","number":"12 pt A","starting_page":"1881","ending_page":"1892","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbalip.2016.09.008"],"issn":["1388-1981"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2008645","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/27877903","label":"url"},{"@id":"https://www.scopus.com/pages/publications/85019070861","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=317627","label":"url"}],"paper_title":{"en":"The novel functional nucleic acid iRed effectively regulates target genes following cytoplasmic delivery by faint electric treatment","ja":"The novel functional nucleic acid iRed effectively regulates target genes following cytoplasmic delivery by faint electric treatment"},"authors":{"en":[{"name":"Hasan Mahadi"},{"name":"Saito-Tarashima Noriko"},{"name":"Fujikawa Koki"},{"name":"Ohgita Takashi"},{"name":"Hama Susumu"},{"name":"Tanaka Tamotsu"},{"name":"Saito Hiroyuki"},{"name":"Minakawa Noriaki"},{"name":"Kogure Kentaro"}],"ja":[{"name":"Hasan Mahadi"},{"name":"田良島 典子"},{"name":"Fujikawa Koki"},{"name":"Ohgita Takashi"},{"name":"Hama Susumu"},{"name":"田中 保"},{"name":"斎藤 博幸"},{"name":"南川 典昭"},{"name":"小暮 健太朗"}]},"description":{"en":"An intelligent shRNA expression device (iRed) contains the minimum essential components needed for shRNA production in cells, and could be a novel tool to regulate target genes. However, general delivery carriers consisting of cationic polymers/lipids could impede function of a newly generated shRNA via electrostatic interaction in the cytoplasm. Recently, we found that faint electric treatment (fET) of cells enhanced delivery of siRNA and functional nucleic acids into the cytoplasm in the absence of delivery carriers. Here, we examined fET of cells stably expressing luciferase in the presence of iRed encoding anti-luciferase shRNA. Transfection of lipofectamine 2000 (LFN)/iRed lipoplexes showed an RNAi effect, but fET-mediated iRed transfection did not, likely because of the endosomal localization of iRed after delivery. However, fET in the presence of lysosomotropic agent chloroquine significantly improved the RNAi effect of iRed/fET to levels that were higher than those for the LFN/iRed lipoplexes. Furthermore, the amount of lipid droplets in adipocytes significantly decreased following fET with iRed against resistin in the presence of chloroquine. Thus, iRed could be a useful tool to regulate target genes following fET-mediated cytoplasmic delivery with endosomal escape devices.","ja":"An intelligent shRNA expression device (iRed) contains the minimum essential components needed for shRNA production in cells, and could be a novel tool to regulate target genes. However, general delivery carriers consisting of cationic polymers/lipids could impede function of a newly generated shRNA via electrostatic interaction in the cytoplasm. Recently, we found that faint electric treatment (fET) of cells enhanced delivery of siRNA and functional nucleic acids into the cytoplasm in the absence of delivery carriers. Here, we examined fET of cells stably expressing luciferase in the presence of iRed encoding anti-luciferase shRNA. Transfection of lipofectamine 2000 (LFN)/iRed lipoplexes showed an RNAi effect, but fET-mediated iRed transfection did not, likely because of the endosomal localization of iRed after delivery. However, fET in the presence of lysosomotropic agent chloroquine significantly improved the RNAi effect of iRed/fET to levels that were higher than those for the LFN/iRed lipoplexes. Furthermore, the amount of lipid droplets in adipocytes significantly decreased following fET with iRed against resistin in the presence of chloroquine. Thus, iRed could be a useful tool to regulate target genes following fET-mediated cytoplasmic delivery with endosomal escape devices."},"publication_date":"2016-08-04","publication_name":{"en":"Science and Technology of Advanced Materials","ja":"Science and Technology of Advanced Materials"},"volume":"17","number":"17","starting_page":"554","ending_page":"562","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1080/14686996.2016.1221726"],"issn":["1468-6996"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/27421691","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84978805217","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=328245","label":"url"}],"paper_title":{"en":"Preferable existence of polyunsaturated lysophosphatidic acids in human follicular fluid from patients programmed with in vitro fertilization.","ja":"Preferable existence of polyunsaturated lysophosphatidic acids in human follicular fluid from patients programmed with in vitro fertilization."},"authors":{"en":[{"name":"Yamamoto Junpei"},{"name":"Omura Midori"},{"name":"Tuchiya Koichiro"},{"name":"Hidaka Mayumi"},{"name":"Kuwahara Akira"},{"name":"Irahara Minoru"},{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"}],"ja":[{"name":"Yamamoto Junpei"},{"name":"Omura Midori"},{"name":"Tuchiya Koichiro"},{"name":"Hidaka Mayumi"},{"name":"桑原 章"},{"name":"苛原 稔"},{"name":"田中 保"},{"name":"德村 彰"}]},"description":{"en":"Lysophosphatidic acid (LPA) exerts diverse physiological effects on various types of animal cells, including reproductive cells, through its binding to six LPA receptors. We previously found that LPA promoted maturation of the nucleus and cytoplasm of mouse and hamster oocytes surrounded by cumulus cells in vitro. Using gas-liquid chromatography, we previously reported detection of several species of LPA by analyzing the fatty acid methyl esters derived from thin layer chromatography-purified LPA in lipid extract from incubated follicular fluids programmed with in vitro fertilization. In this study using liquid chromatography- tandem mass spectrometry, we directly detected high levels of linoleoyl, arachidonoyl, and docosahexaenoyl LPAs in human follicular fluid. This unique molecular species composition of LPA was suggested to be due to a balance between the low LPA-degrading activity and high LPA-producing activity of autotaxin in human follicular fluid. Our results suggest that polyunsaturated LPAs produced by autotaxin in human follicular fluid exert unknown physiological effects on cumulus cells.","ja":"Lysophosphatidic acid (LPA) exerts diverse physiological effects on various types of animal cells, including reproductive cells, through its binding to six LPA receptors. We previously found that LPA promoted maturation of the nucleus and cytoplasm of mouse and hamster oocytes surrounded by cumulus cells in vitro. Using gas-liquid chromatography, we previously reported detection of several species of LPA by analyzing the fatty acid methyl esters derived from thin layer chromatography-purified LPA in lipid extract from incubated follicular fluids programmed with in vitro fertilization. In this study using liquid chromatography- tandem mass spectrometry, we directly detected high levels of linoleoyl, arachidonoyl, and docosahexaenoyl LPAs in human follicular fluid. This unique molecular species composition of LPA was suggested to be due to a balance between the low LPA-degrading activity and high LPA-producing activity of autotaxin in human follicular fluid. Our results suggest that polyunsaturated LPAs produced by autotaxin in human follicular fluid exert unknown physiological effects on cumulus cells."},"publication_date":"2016-07-12","publication_name":{"en":"Prostaglandins & Other Lipid Mediators","ja":"Prostaglandins & Other Lipid Mediators"},"volume":"126","starting_page":"16","ending_page":"23","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.prostaglandins.2016.07.008"],"issn":["1098-8823"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/27267499","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84975841169","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=332879","label":"url"}],"paper_title":{"en":"Reduced rat plasma lysophosphatidylglycerol or lysophosphatidic acid level as a biomarker of aristolochic acid-induced renal and adipose dysfunctions.","ja":"Reduced rat plasma lysophosphatidylglycerol or lysophosphatidic acid level as a biomarker of aristolochic acid-induced renal and adipose dysfunctions."},"authors":{"en":[{"name":"Tsutsumi Toshihiko"},{"name":"Okamoto Yoko"},{"name":"Yamakawa Syougo"},{"name":"Bingjun Cheng"},{"name":"Ishihara Akira"},{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"}],"ja":[{"name":"Tsutsumi Toshihiko"},{"name":"Okamoto Yoko"},{"name":"Yamakawa Syougo"},{"name":"Bingjun Cheng"},{"name":"Ishihara Akira"},{"name":"田中 保"},{"name":"德村 彰"}]},"description":{"en":"Food products and diet pills containing aristolochic acid (AA) are responsible for a rapid progression of nephropathy associated with reduced body weight in human beings. In this study, we investigated the relationship of dietary NaCl and lysophospholipid (LPL) plasma levels to body weight gain in AA-treated rats. Male rats receiving a salt-deficient chow, normal salt chow or high salt chow were injected intraperitoneally daily with AA for 15days. Body weight, visceral fat mass, food intake, levels of LPL in plasma and its synthesized enzyme were investigated. Body weight gain, visceral fat mass and daily food intake were smaller in AA-treated rats than those of control rats, regardless of dietary salt concentration. AA treatment decreased plasma levels of major lysophosphatidic acid (LPA) molecular species in rats fed the normal or high-salt chow but not the salt-deficient chow, whereas both the plasma lysophospholipase D activity and kidney mRNA level of autotaxin of AA-treated rats fed chow with defined salt concentrations were lower than those of control rats. Plasma levels of major molecular species of lysophosphatidylglycerol (LPG) in AA-treated rat groups fed chow with defined salt concentrations were lower than those of control rats. Plasma levels of LPG and LPA seem to be relevant to the reduced body weight gain and fat mass due to AA treatment.","ja":"Food products and diet pills containing aristolochic acid (AA) are responsible for a rapid progression of nephropathy associated with reduced body weight in human beings. In this study, we investigated the relationship of dietary NaCl and lysophospholipid (LPL) plasma levels to body weight gain in AA-treated rats. Male rats receiving a salt-deficient chow, normal salt chow or high salt chow were injected intraperitoneally daily with AA for 15days. Body weight, visceral fat mass, food intake, levels of LPL in plasma and its synthesized enzyme were investigated. Body weight gain, visceral fat mass and daily food intake were smaller in AA-treated rats than those of control rats, regardless of dietary salt concentration. AA treatment decreased plasma levels of major lysophosphatidic acid (LPA) molecular species in rats fed the normal or high-salt chow but not the salt-deficient chow, whereas both the plasma lysophospholipase D activity and kidney mRNA level of autotaxin of AA-treated rats fed chow with defined salt concentrations were lower than those of control rats. Plasma levels of major molecular species of lysophosphatidylglycerol (LPG) in AA-treated rat groups fed chow with defined salt concentrations were lower than those of control rats. Plasma levels of LPG and LPA seem to be relevant to the reduced body weight gain and fat mass due to AA treatment."},"publication_date":"2016-06-04","publication_name":{"en":"Life Sciences","ja":"Life Sciences"},"volume":"157","starting_page":"208","ending_page":"216","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.lfs.2016.06.003"],"issn":["1879-0631"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1390001205191889280/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=310728","label":"url"}],"paper_title":{"en":"食品に含まれるグリコシルイノシトールホスホセラミドおよびフィトセラミド-1-リン酸","ja":"食品に含まれるグリコシルイノシトールホスホセラミドおよびフィトセラミド-1-リン酸"},"authors":{"en":[{"name":"喜田 孝史"},{"name":"木村 朱里"},{"name":"伊藤 葵"},{"name":"山下 量平"},{"name":"Kogure Kentaro"},{"name":"Tokumura Akira"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"喜田 孝史"},{"name":"木村 朱里"},{"name":"伊藤 葵"},{"name":"山下 量平"},{"name":"小暮 健太朗"},{"name":"德村 彰"},{"name":"田中 保"}]},"publication_date":"2016","publication_name":{"en":"Journal of Lipid Nutrition","ja":"脂質栄養学"},"volume":"25","starting_page":"75","ending_page":"85","languages":["jpn"],"referee":true,"identifiers":{"doi":["10.4010/jln.25.75"],"issn":["1343-4594"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/26694604","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84957439211","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=310727","label":"url"}],"paper_title":{"en":"Analysis of molecular species profiles of ceramide-1-phosphate and sphingomyelin using MALDI-TOF mass spectrometry","ja":"Analysis of molecular species profiles of ceramide-1-phosphate and sphingomyelin using MALDI-TOF mass spectrometry"},"authors":{"en":[{"name":"Yamashita Ryouhei"},{"name":"Tabata Yumika"},{"name":"Iga Erina"},{"name":"Nakao Michiyasu"},{"name":"Sano Shigeki"},{"name":"Kogure Kentaro"},{"name":"Tokumura Akira"},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Yamashita Ryouhei"},{"name":"Tabata Yumika"},{"name":"Iga Erina"},{"name":"中尾 允泰"},{"name":"佐野 茂樹"},{"name":"小暮 健太朗"},{"name":"德村 彰"},{"name":"田中 保"}]},"description":{"en":"Ceramide-1-phosphate (C1P) is a potential signaling molecule that modulates various cellular functions in animals. It has been known that C1P with different N-acyl lengths induce biological responses differently. However, molecular species profiles of the C1P in animal tissues have not been extensively examined yet. Here, we developed a method for determination of the molecular species of a C1P using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with Phos-tag, a phosphate capture molecule. The amounts of total C1P in skin, brain, liver, kidney and small intestine of mice were determined to be 344, 151, 198, 96 and 90 pmol/g wet weight, respectively. We found a C1P species having an α-hydroxypalmitoyl residue (h-C1P, 44 pmol/g wet weight) in mouse skin. The h-C1P was detected only in the skin, and not other tissues of mice. The same analysis was applied to sphingomyelin after conversion of sphingomyelin to C1P by Streptomyces chromofuscus phospholipase D. We found that molecular species profiles of sphingomyelin in skin, kidney and small intestine of mice were similar to those of C1P in corresponding tissues. In contrast, molecular species profiles of sphingomyelin in liver and brain were quite different from those of C1P in these tissues, indicating selective synthesis or degradation of C1P in these tissues. The method described here will be useful for detection of changes in molecular species profiles of C1P and sphingomyelin.","ja":"Ceramide-1-phosphate (C1P) is a potential signaling molecule that modulates various cellular functions in animals. It has been known that C1P with different N-acyl lengths induce biological responses differently. However, molecular species profiles of the C1P in animal tissues have not been extensively examined yet. Here, we developed a method for determination of the molecular species of a C1P using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with Phos-tag, a phosphate capture molecule. The amounts of total C1P in skin, brain, liver, kidney and small intestine of mice were determined to be 344, 151, 198, 96 and 90 pmol/g wet weight, respectively. We found a C1P species having an α-hydroxypalmitoyl residue (h-C1P, 44 pmol/g wet weight) in mouse skin. The h-C1P was detected only in the skin, and not other tissues of mice. The same analysis was applied to sphingomyelin after conversion of sphingomyelin to C1P by Streptomyces chromofuscus phospholipase D. We found that molecular species profiles of sphingomyelin in skin, kidney and small intestine of mice were similar to those of C1P in corresponding tissues. In contrast, molecular species profiles of sphingomyelin in liver and brain were quite different from those of C1P in these tissues, indicating selective synthesis or degradation of C1P in these tissues. The method described here will be useful for detection of changes in molecular species profiles of C1P and sphingomyelin."},"publication_date":"2016","publication_name":{"en":"Lipids","ja":"Lipids"},"volume":"51","number":"2","starting_page":"263","ending_page":"270","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s11745-015-4082-0"],"issn":["1558-9307"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2012754","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84924599379","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=319904","label":"url"}],"paper_title":{"en":"Reduced kidney levels of lysophosphatidic acids in rats after chronic administration of aristolochic acid: Its possible protective role in renal fibrosis","ja":"Reduced kidney levels of lysophosphatidic acids in rats after chronic administration of aristolochic acid: Its possible protective role in renal fibrosis"},"authors":{"en":[{"name":"Tsutsumi Toshihiko"},{"name":"Yamakawa Syougo"},{"name":"Ishihara Akira"},{"name":"Yamamoto Aimi"},{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"}],"ja":[{"name":"Tsutsumi Toshihiko"},{"name":"Yamakawa Syougo"},{"name":"Ishihara Akira"},{"name":"Yamamoto Aimi"},{"name":"田中 保"},{"name":"德村 彰"}]},"publication_date":"2015-02","publication_name":{"en":"Toxicology Reports","ja":"Toxicology Reports"},"volume":"2","starting_page":"121","ending_page":"129","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.toxrep.2015.02.012"],"issn":["2214-7500"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/24641902","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84899540615","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=303430","label":"url"}],"paper_title":{"en":"Potentials of the circulating pruritogenic mediator lysophosphatidic acid in development of allergic skin inflammation in mice: role of blood cell-associated lysophospholipase D activity of autotaxin.","ja":"Potentials of the circulating pruritogenic mediator lysophosphatidic acid in development of allergic skin inflammation in mice: role of blood cell-associated lysophospholipase D activity of autotaxin."},"authors":{"en":[{"name":"Shimizu Yoshibumi"},{"name":"Morikawa Yoshiyuki"},{"name":"Okudaira Shinichi"},{"name":"Kimoto Shigenobu"},{"name":"Tanaka Tamotsu"},{"name":"Aoki Junken"},{"name":"Tokumura Akira"}],"ja":[{"name":"Shimizu Yoshibumi"},{"name":"Morikawa Yoshiyuki"},{"name":"Okudaira Shinichi"},{"name":"Kimoto Shigenobu"},{"name":"田中 保"},{"name":"Aoki Junken"},{"name":"德村 彰"}]},"description":{"en":"Itching and infiltration of immune cells are important hallmarks of atopic dermatitis (AD). Although various studies have focused on peripheral mediator-mediated mechanisms, systemic mediator-mediated mechanisms are also important in the pathogenesis and development of AD. Herein, we found that intradermal injection of lysophosphatidic acid (LPA), a bioactive phospholipid, induces scratching responses by Institute of Cancer Research mice through LPA1 receptor- and opioid μ receptor-mediating mechanisms, indicating its potential as a pruritogen. The circulating level of LPA in Naruto Research Institute Otsuka Atrichia mice, a systemic AD model, with severe scratching was found to be higher than that of control BALB/c mice, probably because of the increased lysophospholipase D activity of autotaxin (ATX) in the blood (mainly membrane associated) rather than in plasma (soluble). Heparan sulfate proteoglycan was shown to be involved in the association of ATX with blood cells. The sequestration of ATX protein on the blood cells by heparan sulfate proteoglycan may accelerate the transport of LPA to the local apical surface of vascular endothelium with LPA receptors, promoting the hyperpermeability of venules and the pathological uptake of immune cells, aggravating lesion progression and itching in Naruto Research Institute Otsuka Atrichia mice.","ja":"Itching and infiltration of immune cells are important hallmarks of atopic dermatitis (AD). Although various studies have focused on peripheral mediator-mediated mechanisms, systemic mediator-mediated mechanisms are also important in the pathogenesis and development of AD. Herein, we found that intradermal injection of lysophosphatidic acid (LPA), a bioactive phospholipid, induces scratching responses by Institute of Cancer Research mice through LPA1 receptor- and opioid μ receptor-mediating mechanisms, indicating its potential as a pruritogen. The circulating level of LPA in Naruto Research Institute Otsuka Atrichia mice, a systemic AD model, with severe scratching was found to be higher than that of control BALB/c mice, probably because of the increased lysophospholipase D activity of autotaxin (ATX) in the blood (mainly membrane associated) rather than in plasma (soluble). Heparan sulfate proteoglycan was shown to be involved in the association of ATX with blood cells. The sequestration of ATX protein on the blood cells by heparan sulfate proteoglycan may accelerate the transport of LPA to the local apical surface of vascular endothelium with LPA receptors, promoting the hyperpermeability of venules and the pathological uptake of immune cells, aggravating lesion progression and itching in Naruto Research Institute Otsuka Atrichia mice."},"publication_date":"2014-05","publication_name":{"en":"The American Journal of Pathology","ja":"The American Journal of Pathology"},"volume":"184","number":"5","starting_page":"1593","ending_page":"1603","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.ajpath.2014.01.029"],"issn":["1525-2191"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/24659112","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84900792021","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=303429","label":"url"}],"paper_title":{"en":"Metabolic conversion of C20 polymethylene-interrupted polyunsaturated fatty acids to essential fatty acids.","ja":"Metabolic conversion of C20 polymethylene-interrupted polyunsaturated fatty acids to essential fatty acids."},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Uozumi Sachika"},{"name":"Morito Katsuya"},{"name":"Osumi Takashi"},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Uozumi Sachika"},{"name":"Morito Katsuya"},{"name":"Osumi Takashi"},{"name":"德村 彰"}]},"description":{"en":"Polymethylene-interrupted (PMI)-polyunsaturated fatty acids (PUFA) are fatty acids present largely in gymnosperm. Sciadonic acid (SciA, 20:3 Δ-5,11,14) and juniperonic acid (JA, 20:4 Δ-5,11,14,17) are typical C20 PMI-PUFA with an isolated double bond at Δ5. Previously, we found that SciA and JA are converted to linoleic acid (LNA) and α-linolenic acid (ΑLA), respectively. The conversion process includes chain-shortening step by peroxisomal β-oxidation for elimination a double bond at Δ5, and subsequent chain-elongation step in microsomes. In this study, we examined the substrate specificity of this metabolism in rodent and human cells. Supplementation of SciA, eicosadienoic acid (EDA, 20:2 Δ-11,14) or JA to CHO-K1 cells (wild type) induced an accumulation of LNA, LNA or ALA, respectively, in cellular lipids. These changes were not observed in the peroxisomes-deficient CHO cells, indicating involvement of peroxisomes in the metabolism. Two types of human cells (MKN74 and HepG2) also converted the C20 PMI-PUFA and EDA to the respective essential fatty acids. In contrast, no chain-shortened metabolite of pinolenic acid (18:3 Δ-5,9,12) was detected in any cell lines tested. From these results, C20 PMI-PUFA and EDA, but not C18 PMI-PUFA, are suggested as being effectively converted to essential fatty acids by the fatty acid remodeling system in rodent and human cells.","ja":"Polymethylene-interrupted (PMI)-polyunsaturated fatty acids (PUFA) are fatty acids present largely in gymnosperm. Sciadonic acid (SciA, 20:3 Δ-5,11,14) and juniperonic acid (JA, 20:4 Δ-5,11,14,17) are typical C20 PMI-PUFA with an isolated double bond at Δ5. Previously, we found that SciA and JA are converted to linoleic acid (LNA) and α-linolenic acid (ΑLA), respectively. The conversion process includes chain-shortening step by peroxisomal β-oxidation for elimination a double bond at Δ5, and subsequent chain-elongation step in microsomes. In this study, we examined the substrate specificity of this metabolism in rodent and human cells. Supplementation of SciA, eicosadienoic acid (EDA, 20:2 Δ-11,14) or JA to CHO-K1 cells (wild type) induced an accumulation of LNA, LNA or ALA, respectively, in cellular lipids. These changes were not observed in the peroxisomes-deficient CHO cells, indicating involvement of peroxisomes in the metabolism. Two types of human cells (MKN74 and HepG2) also converted the C20 PMI-PUFA and EDA to the respective essential fatty acids. In contrast, no chain-shortened metabolite of pinolenic acid (18:3 Δ-5,9,12) was detected in any cell lines tested. From these results, C20 PMI-PUFA and EDA, but not C18 PMI-PUFA, are suggested as being effectively converted to essential fatty acids by the fatty acid remodeling system in rodent and human cells."},"publication_date":"2014-05","publication_name":{"en":"Lipids","ja":"Lipids"},"volume":"49","number":"5","starting_page":"423","ending_page":"429","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s11745-014-3896-5"],"issn":["1558-9307"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/24375908","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84902549036","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=272305","label":"url"}],"paper_title":{"en":"Type 2 lysophosphatidic acid receptor in gastric surface mucous cells: Possible implication of prostaglandin E2 production","ja":"Type 2 lysophosphatidic acid receptor in gastric surface mucous cells: Possible implication of prostaglandin E2 production"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Ohmoto Mayumi"},{"name":"Morito Katsuya"},{"name":"Kondo H."},{"name":"Urikura Mai"},{"name":"Satouchi Kiyoshi"},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Ohmoto Mayumi"},{"name":"Morito Katsuya"},{"name":"Kondo H."},{"name":"Urikura Mai"},{"name":"Satouchi Kiyoshi"},{"name":"德村 彰"}]},"description":{"en":"Lysophosphatidic acid (LPA) is a lipid mediator that induces various cell responses via its specific receptors. Recently, we found that orally administered LPA and phosphatidic acid (PA) ameliorate stress- or aspirin-induced stomach injury. However, the mechanisms underlying these effects have not been elucidated yet. In this study, we examined effect of LPA on prostaglandin (PG) E2 production in MKN74 cells, a gastric cell-line expressing type 2 LPA receptor (LPA2). When the cells were treated with LPA, the level of mRNA of COX-2 but not COX-1 was upregulated. The LPA effect was abolished when the cells were pretreated with pertussis toxin (PTX), suggesting the involvement of receptor(s) coupled with Gi. Pretreatment of MKN74 cells with LPA enhanced the PGE2 production triggered by calcium ionophore A23187. Again, PTX abolished the LPA effect. Fluorescent immunohistochemistry using an antibody against LPA2 showed that surface mucous cells (pit cells) in gastric mucosa of mice express LPA2 on the apical side of the plasma membrane. These results suggest that LPA in the diet or its digestion may contribute to the epithelial integrity of stomach mucosa by enhancement of PGE2 production via activation of LPA2. © 2013 BioFactors, 2013.","ja":"Lysophosphatidic acid (LPA) is a lipid mediator that induces various cell responses via its specific receptors. Recently, we found that orally administered LPA and phosphatidic acid (PA) ameliorate stress- or aspirin-induced stomach injury. However, the mechanisms underlying these effects have not been elucidated yet. In this study, we examined effect of LPA on prostaglandin (PG) E2 production in MKN74 cells, a gastric cell-line expressing type 2 LPA receptor (LPA2). When the cells were treated with LPA, the level of mRNA of COX-2 but not COX-1 was upregulated. The LPA effect was abolished when the cells were pretreated with pertussis toxin (PTX), suggesting the involvement of receptor(s) coupled with Gi. Pretreatment of MKN74 cells with LPA enhanced the PGE2 production triggered by calcium ionophore A23187. Again, PTX abolished the LPA effect. Fluorescent immunohistochemistry using an antibody against LPA2 showed that surface mucous cells (pit cells) in gastric mucosa of mice express LPA2 on the apical side of the plasma membrane. These results suggest that LPA in the diet or its digestion may contribute to the epithelial integrity of stomach mucosa by enhancement of PGE2 production via activation of LPA2. © 2013 BioFactors, 2013."},"publication_date":"2014-05","publication_name":{"en":"BioFactors","ja":"BioFactors"},"volume":"40","number":"3","starting_page":"355","ending_page":"361","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1002/biof.1147"],"issn":["1872-8081"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/24582488","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84897115979","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=279691","label":"url"}],"paper_title":{"en":"Increased lysophospholipase D activity of autotaxin in sera of patients with atopic dermatitis.","ja":"Increased lysophospholipase D activity of autotaxin in sera of patients with atopic dermatitis."},"authors":{"en":[{"name":"Shimizu Yoshibumi"},{"name":"Murao Kazutoshi"},{"name":"Tanaka Tamotsu"},{"name":"Kubo Yoshiaki"},{"name":"Tokumura Akira"}],"ja":[{"name":"Shimizu Yoshibumi"},{"name":"村尾 和俊"},{"name":"田中 保"},{"name":"久保 宜明"},{"name":"德村 彰"}]},"publication_date":"2014-02-06","publication_name":{"en":"Journal of Dermatological Science","ja":"Journal of Dermatological Science"},"volume":"74","number":"2","starting_page":"162","ending_page":"165","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.jdermsci.2014.01.010"],"issn":["1873-569X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/23738625","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=272304","label":"url"}],"paper_title":{"en":"Identification of a sphingolipid-specific phospholipase D activity associated with the generation of phytoceramide-1-phosphate in cabbage leaves","ja":"Identification of a sphingolipid-specific phospholipase D activity associated with the generation of phytoceramide-1-phosphate in cabbage leaves"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Kida T."},{"name":"Imai H."},{"name":"Morishige J."},{"name":"Yamashita R."},{"name":"Matsuoka H."},{"name":"Uozumi S."},{"name":"Satouchi K."},{"name":"Nagano M."},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Kida T."},{"name":"Imai H."},{"name":"Morishige J."},{"name":"Yamashita R."},{"name":"Matsuoka H."},{"name":"Uozumi S."},{"name":"Satouchi K."},{"name":"Nagano M."},{"name":"德村 彰"}]},"description":{"en":"The structure and biosynthetic route for an unidentified lipid (lipid X) detected by TLC of cabbage (Brassica oleracea) lipids was determined. Lipid X is a phospholipid that is resistant to mild alkali and detectable by MALDI-TOF MS as an adduct with Phos-tag, a phosphate-capture zinc complex. Various α-hydroxy fatty acids (16:0, 22:0, 24:0 and 24:1) were detected by GC-MS of fatty acid methyl esters prepared from lipid X. The deacyl derivative of lipid X was determined to be 4-hydroxysphingenine (dehydrophytosphingosine)-1-phosphate by MALDI-TOF MS with Phos-tag. From these results, lipid X was determined to be phytoceramide-1-phosphate (PC1P) with an α-hydroxy fatty acid. When cabbage homogenates were incubated, PC1P was formed, with a concomitant decrease in the amount of glycosylinositol phosphoceramide (GIPC). The formation of PC1P from GIPC was confirmed by treatment of purified cabbage GIPC with a membrane fraction of cabbage homogenates. Using a partially purified enzyme fraction, we found that the enzyme hydrolyzes GIPC specifically, but not glycerophospholipids and sphingomyelin. Arabidopsis thaliana also had this enzyme activity. From these results, we conclude that a previously uncharacterized phospholipase D activity that specifically hydrolyzes GIPC produces PC1P in brassicaceous plants.","ja":"The structure and biosynthetic route for an unidentified lipid (lipid X) detected by TLC of cabbage (Brassica oleracea) lipids was determined. Lipid X is a phospholipid that is resistant to mild alkali and detectable by MALDI-TOF MS as an adduct with Phos-tag, a phosphate-capture zinc complex. Various α-hydroxy fatty acids (16:0, 22:0, 24:0 and 24:1) were detected by GC-MS of fatty acid methyl esters prepared from lipid X. The deacyl derivative of lipid X was determined to be 4-hydroxysphingenine (dehydrophytosphingosine)-1-phosphate by MALDI-TOF MS with Phos-tag. From these results, lipid X was determined to be phytoceramide-1-phosphate (PC1P) with an α-hydroxy fatty acid. When cabbage homogenates were incubated, PC1P was formed, with a concomitant decrease in the amount of glycosylinositol phosphoceramide (GIPC). The formation of PC1P from GIPC was confirmed by treatment of purified cabbage GIPC with a membrane fraction of cabbage homogenates. Using a partially purified enzyme fraction, we found that the enzyme hydrolyzes GIPC specifically, but not glycerophospholipids and sphingomyelin. Arabidopsis thaliana also had this enzyme activity. From these results, we conclude that a previously uncharacterized phospholipase D activity that specifically hydrolyzes GIPC produces PC1P in brassicaceous plants."},"publication_date":"2013-07-05","publication_name":{"en":"The FEBS Journal","ja":"The FEBS Journal"},"volume":"280","number":"16","starting_page":"3797","ending_page":"3809","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1111/febs.12374"],"issn":["1742-4658"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/23161268","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=272303","label":"url"}],"paper_title":{"en":"Orally administered phosphatidic acids and lysophosphatidic acids ameliorate aspirin-induced stomach mucosal injury in mice","ja":"Orally administered phosphatidic acids and lysophosphatidic acids ameliorate aspirin-induced stomach mucosal injury in mice"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Morito K."},{"name":"Kinoshita M."},{"name":"Ohmoto M."},{"name":"Urikura M."},{"name":"Satouchi K."},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Morito K."},{"name":"Kinoshita M."},{"name":"Ohmoto M."},{"name":"Urikura M."},{"name":"Satouchi K."},{"name":"德村 彰"}]},"description":{"en":"Recent investigations revealed that lysophosphatidic acid (LPA), a phospholipid with a growth factor-like activity, plays an important role in the integrity of the gastrointestinal tract epithelium. This paper attempts to clarify the effect of orally administered phosphatidic acid (PA) and LPA on aspirin-induced gastric lesions in mice. Phospholipids, a free fatty acid, a diacylglycerol and a triglyceride at 1 mM (5.7 μmol/kg body weight) or 0.1 mM were orally administered to mice 0.5 h before oral administration of aspirin (1.7 mmol/kg). The total length of lesions formed on the stomach wall was measured as a lesion index. Formation of LPA from PA in the mouse stomach was examined by in vitro (in stomach lavage fluid), ex vivo (in an isolated stomach) and in vivo (in the stomach of a living mouse) examinations of phospholipase activity. Palmitic acid, dioleoyl-glycerol, olive oil and lysophosphatidylcholine did not affect the aspirin-induced lesions. In contrast, phosphatidylcholine (1 mM), LPA (1 mM) and PA (0.1, 1 mM) significantly reduced the lesion index. Evidence for formation of LPA from PA in the stomach by gastric phospholipase A2 was obtained by in vitro, ex vivo and in vivo experiments. An LPA-specific receptor, LPA2, was found to be localized on the gastric surface-lining cells of mice. Pretreatment with PA-rich diets may prevent nonsteroidal anti-inflammatory drug-induced stomach ulcers.","ja":"Recent investigations revealed that lysophosphatidic acid (LPA), a phospholipid with a growth factor-like activity, plays an important role in the integrity of the gastrointestinal tract epithelium. This paper attempts to clarify the effect of orally administered phosphatidic acid (PA) and LPA on aspirin-induced gastric lesions in mice. Phospholipids, a free fatty acid, a diacylglycerol and a triglyceride at 1 mM (5.7 μmol/kg body weight) or 0.1 mM were orally administered to mice 0.5 h before oral administration of aspirin (1.7 mmol/kg). The total length of lesions formed on the stomach wall was measured as a lesion index. Formation of LPA from PA in the mouse stomach was examined by in vitro (in stomach lavage fluid), ex vivo (in an isolated stomach) and in vivo (in the stomach of a living mouse) examinations of phospholipase activity. Palmitic acid, dioleoyl-glycerol, olive oil and lysophosphatidylcholine did not affect the aspirin-induced lesions. In contrast, phosphatidylcholine (1 mM), LPA (1 mM) and PA (0.1, 1 mM) significantly reduced the lesion index. Evidence for formation of LPA from PA in the stomach by gastric phospholipase A2 was obtained by in vitro, ex vivo and in vivo experiments. An LPA-specific receptor, LPA2, was found to be localized on the gastric surface-lining cells of mice. Pretreatment with PA-rich diets may prevent nonsteroidal anti-inflammatory drug-induced stomach ulcers."},"publication_date":"2013","publication_name":{"en":"Digestive Diseases and Sciences","ja":"Digestive Diseases and Sciences"},"volume":"58","number":"4","starting_page":"950","ending_page":"958","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s10620-012-2475-y"],"issn":["1573-2568"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/23098184","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=270851","label":"url"}],"paper_title":{"en":"Phosphatidic acid production in the processing of cabbage leaves","ja":"Phosphatidic acid production in the processing of cabbage leaves"},"authors":{"en":[{"name":"Urikura, Mai"},{"name":"Morishige Jun-ichi"},{"name":"Tanaka Tamotsu"},{"name":"Satouchi Kiyoshi"}],"ja":[{"name":"Urikura, Mai"},{"name":"Morishige Jun-ichi"},{"name":"田中 保"},{"name":"Satouchi Kiyoshi"}]},"description":{"en":"Lysophosphatidic acid (LPA) is a lipid mediator involved in various physiological responses, including wound healing. Evidence of the antiulcer activity of LPA has been reported, and soybean LPA at a concentration of 10 μM is effective in reducing stress-induced gastric ulcer. Because LPA can be formed from phosphatidic acid (PA) by digestive phospholipase A2, dietary PA can be considered a potential antiulcer phospholipid. In this study, PA production in cut processing of cabbage leaves was examined. The amounts of PA in sliced, minced, and homogenized cabbage leaves were 107 ± 5, 134 ± 19, and 286 ± 29 nmol PA/g (wet weight), respectively, all being significantly higher than the amount of PA found in intact leaves. Mixing mayonnaise with sliced cabbage dramatically increased the PA content (1586 ± 393 nmol/3 g), indicating phospholipase D activity leaked raw cabbage produced PA. These results indicate that fine cutting raw cabbage leaves and mixing them with foods rich in phospholipids resulted in an abundant production of PA.","ja":"Lysophosphatidic acid (LPA) is a lipid mediator involved in various physiological responses, including wound healing. Evidence of the antiulcer activity of LPA has been reported, and soybean LPA at a concentration of 10 μM is effective in reducing stress-induced gastric ulcer. Because LPA can be formed from phosphatidic acid (PA) by digestive phospholipase A2, dietary PA can be considered a potential antiulcer phospholipid. In this study, PA production in cut processing of cabbage leaves was examined. The amounts of PA in sliced, minced, and homogenized cabbage leaves were 107 ± 5, 134 ± 19, and 286 ± 29 nmol PA/g (wet weight), respectively, all being significantly higher than the amount of PA found in intact leaves. Mixing mayonnaise with sliced cabbage dramatically increased the PA content (1586 ± 393 nmol/3 g), indicating phospholipase D activity leaked raw cabbage produced PA. These results indicate that fine cutting raw cabbage leaves and mixing them with foods rich in phospholipids resulted in an abundant production of PA."},"publication_date":"2012-11-01","publication_name":{"en":"Journal of Agricultural and Food Chemistry","ja":"Journal of Agricultural and Food Chemistry"},"volume":"60","number":"45","starting_page":"11359","ending_page":"11365","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1021/jf303515z"],"issn":["1520-5118"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/22475031","label":"url"},{"@id":"https://www.scopus.com/pages/publications/84860316722","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=255744","label":"url"}],"paper_title":{"en":"Quantification of phosphatidic acid in foodstuffs using TLC-imaging technique","ja":"Quantification of phosphatidic acid in foodstuffs using TLC-imaging technique"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Kassai Ayaka"},{"name":"Ohmoto Mayumi"},{"name":"Morito Katsuya"},{"name":"Kashiwada Yoshiki"},{"name":"Takaishi Yoshihisa"},{"name":"Urikura Mai"},{"name":"Morishige Jun-ichi"},{"name":"Satouchi Kiyoshi"},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Kassai Ayaka"},{"name":"Ohmoto Mayumi"},{"name":"Morito Katsuya"},{"name":"柏田 良樹"},{"name":"高石 喜久"},{"name":"Urikura Mai"},{"name":"Morishige Jun-ichi"},{"name":"Satouchi Kiyoshi"},{"name":"德村 彰"}]},"description":{"en":"Apical application of lysophosphatidic acid (LPA), a growth-factor-like phospholipid, was shown to prevent or restore gastrointestinal (GI) disorders, such as diarrhea and stomach ulcer, in experimental animals. Because LPA is formed from phosphatidic acid (PA) by the activity of digestive phospholipase A(2), PA is a potential component for dietary treatment of such GI disorders. Here, we quantified PA contained in 38 foodstuffs and 3 herbs by a thin-layer-chromatography-imaging technique. Vegetables belonging to Brassicaceae, such as cabbage leaves (700 nmol/g of wet weight) and Japanese radish leaves (570 nmol/g), contained higher amounts of PA than other foodstuffs. Amounts of PA in fruits, cereals, and starchy root vegetables were below 300 nmol/g. Animal foodstuffs contained low amounts of PA (<60 nmol/g). Interestingly, leaves of Mallotus japonicas, a Japanese edible herb used for treatment of stomach ulcer, had the highest PA (1410 nmol/g) among those examined. The data shown here will be useful for the development of dietary treatment for a damaged GI tract.","ja":"Apical application of lysophosphatidic acid (LPA), a growth-factor-like phospholipid, was shown to prevent or restore gastrointestinal (GI) disorders, such as diarrhea and stomach ulcer, in experimental animals. Because LPA is formed from phosphatidic acid (PA) by the activity of digestive phospholipase A(2), PA is a potential component for dietary treatment of such GI disorders. Here, we quantified PA contained in 38 foodstuffs and 3 herbs by a thin-layer-chromatography-imaging technique. Vegetables belonging to Brassicaceae, such as cabbage leaves (700 nmol/g of wet weight) and Japanese radish leaves (570 nmol/g), contained higher amounts of PA than other foodstuffs. Amounts of PA in fruits, cereals, and starchy root vegetables were below 300 nmol/g. Animal foodstuffs contained low amounts of PA (<60 nmol/g). Interestingly, leaves of Mallotus japonicas, a Japanese edible herb used for treatment of stomach ulcer, had the highest PA (1410 nmol/g) among those examined. The data shown here will be useful for the development of dietary treatment for a damaged GI tract."},"publication_date":"2012-04-16","publication_name":{"en":"Journal of Agricultural and Food Chemistry","ja":"Journal of Agricultural and Food Chemistry"},"volume":"60","number":"16","starting_page":"4156","ending_page":"4161","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1021/jf300147y"],"issn":["1520-5118"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"http://id.ndl.go.jp/bib/023553759","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390282679178944384/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=255729","label":"url"}],"paper_title":{"en":"Mass spectrometric analysis of phospholipids with phosphate monoester residue using Phos-tag","ja":"Phos-tagを用いた活性リン脂質の質量分析"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"盛重 純一"},{"name":"瓜倉 真衣"},{"name":"Tokumura Akira"},{"name":"里内 清"}],"ja":[{"name":"田中 保"},{"name":"盛重 純一"},{"name":"瓜倉 真衣"},{"name":"德村 彰"},{"name":"里内 清"}]},"description":{"en":"Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) are growth factor-like bioactive lipids having a phosphate monoester residue. Phos-tag can bind to them and be used both for purification and quantification. In a two-phase solvent system consisting of chloroform/methanol/water, addition of Phos-tag move LPA and S1P from a hydrophilic phase to a hydrophobic phase in the form of their Phos-tag complexes. Using this property, we developed a method for purification of LPA and S1P in biological materials by the phase separation technique. Advantages of use of Phos-tag for detection of LPA and S1P in MALDI-TOF MS are an increase in ionization efficiency and detection as a single-ion form. Homologues of LPA and S1P in natural samples can be quantified by MALDI-TOF MS by using internal standards.<br>","ja":"Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) are growth factor-like bioactive lipids having a phosphate monoester residue. Phos-tag can bind to them and be used both for purification and quantification. In a two-phase solvent system consisting of chloroform/methanol/water, addition of Phos-tag move LPA and S1P from a hydrophilic phase to a hydrophobic phase in the form of their Phos-tag complexes. Using this property, we developed a method for purification of LPA and S1P in biological materials by the phase separation technique. Advantages of use of Phos-tag for detection of LPA and S1P in MALDI-TOF MS are an increase in ionization efficiency and detection as a single-ion form. Homologues of LPA and S1P in natural samples can be quantified by MALDI-TOF MS by using internal standards.<br>"},"publication_date":"2012-01","publication_name":{"en":"SEIBUTSU BUTSURI KAGAKU","ja":"生物物理化学"},"volume":"56","starting_page":"s37","ending_page":"42","languages":["jpn"],"referee":true,"invited":true,"identifiers":{"doi":["10.2198/sbk.56.s37"],"issn":["0031-9082"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/23123475","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=270709","label":"url"}],"paper_title":{"en":"Alterations of plasma levels of lysophosphatidic acid in response to fasting of rats","ja":"Alterations of plasma levels of lysophosphatidic acid in response to fasting of rats"},"authors":{"en":[{"name":"Ino Masaki"},{"name":"Shimizu Yoshibumi"},{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"}],"ja":[{"name":"猪野 真基"},{"name":"清水 嘉文"},{"name":"田中 保"},{"name":"德村 彰"}]},"description":{"en":"The aim of this study was to investigate the effect of fasting on in vivo plasma levels of lysophosphatidic acid (LPA), a physiologically important lysophospholipid mediator. We assayed to measure activities of an LPA-producing enzyme (lysophospholipase D) and LPA-degrading enzyme activities (lysophspholipase A, lipid phosphate phosphatase) in rat plasma or blood, by measuring choline, fatty acid and inorganic phosphate, respectively. Both LPA and its precursor lysophosphatidylcholine (LPC) were quantified by liquid chromatography-tandem mass spectrometry. Fasting of rats for 24 h decreased plasma concentrations of oleoyl-, linoleoyl-, arachidonoyl- and docosahexaenoyl-LPAs, but not palmitoyl- and stearoyl-LPAs, possibly due to decreased levels of corresponding LPCs in the plasma and elevated lipid phosphate phosphatase activity for LPAs in the blood. Our results indicate that the in vivo circulating levels of LPAs in rats are affected by fasting.","ja":"The aim of this study was to investigate the effect of fasting on in vivo plasma levels of lysophosphatidic acid (LPA), a physiologically important lysophospholipid mediator. We assayed to measure activities of an LPA-producing enzyme (lysophospholipase D) and LPA-degrading enzyme activities (lysophspholipase A, lipid phosphate phosphatase) in rat plasma or blood, by measuring choline, fatty acid and inorganic phosphate, respectively. Both LPA and its precursor lysophosphatidylcholine (LPC) were quantified by liquid chromatography-tandem mass spectrometry. Fasting of rats for 24 h decreased plasma concentrations of oleoyl-, linoleoyl-, arachidonoyl- and docosahexaenoyl-LPAs, but not palmitoyl- and stearoyl-LPAs, possibly due to decreased levels of corresponding LPCs in the plasma and elevated lipid phosphate phosphatase activity for LPAs in the blood. Our results indicate that the in vivo circulating levels of LPAs in rats are affected by fasting."},"publication_date":"2012","publication_name":{"en":"Biological & Pharmaceutical Bulletin","ja":"Biological & Pharmaceutical Bulletin"},"volume":"35","number":"11","starting_page":"2059","ending_page":"2063","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1248/bpb.b12-00497"],"issn":["1347-5215"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/21298479","label":"url"},{"@id":"https://www.scopus.com/pages/publications/79960932906","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=372236","label":"url"}],"paper_title":{"en":"Intragastrically administrered lysophospatidic acid protect against gastric ulcer in rats under water-immersion restraint stress","ja":"Intragastrically administrered lysophospatidic acid protect against gastric ulcer in rats under water-immersion restraint stress"},"authors":{"en":[{"name":"Adachi MIka"},{"name":"Horiuchi Gou"},{"name":"Ikematsu Natsuki"},{"name":"Tanaka Tamotsu"},{"name":"Sano Shigeki"},{"name":"Fukuzawa Kenji"},{"name":"Tokumura Akira"}],"ja":[{"name":"足立 美佳"},{"name":"Horiuchi Gou"},{"name":"池松 夏紀"},{"name":"田中 保"},{"name":"佐野 茂樹"},{"name":"福澤 健治"},{"name":"德村 彰"}]},"description":{"en":"Lysophosphatidic acid exerts important physiological effects on many types of animal cells through its specific binding to several G protein-coupled receptors. In particular, its potent wound-healing effect has attracted much attention. To determine whether lysophosphatidic acids in a foodstuff and Chinese medicine are effective in protecting against gastric ulcer, we subjected rats to water-immersion restraint stress. Three direct administrations of a solution of lysophosphatidic acid with a C18 fatty acyl group to the rat stomach in a concentration range of 0.001-0.1 mM resulted in a significant reduction in the number of gastric ulcers induced during water-immersion restraint stress, and the potencies were as follows: linoleoyl species=α-linolenoyl species>oleoyl species. Intragastric administrations of a solution of highly purified lysophosphatidic acid from soybean lecithin significantly protected against the stress-induced gastric ulcers at lower concentrations than partially purified lysophosphatidic acid from soybean lecithin did. In addition, administration of a decocted solution of antyu-san, and lysophosphatidic acid-rich Chinese medicine, to the stomach was more effective in protecting against stress-induced ulcer than decoctations of antyu-san lacking the corydalis tuber component that is rich in lysophosphatidic acid. These results clearly show that lysophosphatidic acid is the effective component of soybean lecithin and antyu-san in protection against stress-induced gastric ulcer in the rat model, and suggest that daily intake of lysophosphatidic acid-rich foods or Chinese medicines may be beneficial for prevention of stress-induced gastric ulcer in human subjects.","ja":"Lysophosphatidic acid exerts important physiological effects on many types of animal cells through its specific binding to several G protein-coupled receptors. In particular, its potent wound-healing effect has attracted much attention. To determine whether lysophosphatidic acids in a foodstuff and Chinese medicine are effective in protecting against gastric ulcer, we subjected rats to water-immersion restraint stress. Three direct administrations of a solution of lysophosphatidic acid with a C18 fatty acyl group to the rat stomach in a concentration range of 0.001-0.1 mM resulted in a significant reduction in the number of gastric ulcers induced during water-immersion restraint stress, and the potencies were as follows: linoleoyl species=α-linolenoyl species>oleoyl species. Intragastric administrations of a solution of highly purified lysophosphatidic acid from soybean lecithin significantly protected against the stress-induced gastric ulcers at lower concentrations than partially purified lysophosphatidic acid from soybean lecithin did. In addition, administration of a decocted solution of antyu-san, and lysophosphatidic acid-rich Chinese medicine, to the stomach was more effective in protecting against stress-induced ulcer than decoctations of antyu-san lacking the corydalis tuber component that is rich in lysophosphatidic acid. These results clearly show that lysophosphatidic acid is the effective component of soybean lecithin and antyu-san in protection against stress-induced gastric ulcer in the rat model, and suggest that daily intake of lysophosphatidic acid-rich foods or Chinese medicines may be beneficial for prevention of stress-induced gastric ulcer in human subjects."},"publication_date":"2011-02-06","publication_name":{"en":"Digestive Diseases and Sciences","ja":"Digestive Diseases and Sciences"},"volume":"56","number":"8","starting_page":"2252","ending_page":"2261","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s10620-011-1595-0"],"issn":["1573-2568"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/20415488","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=210620","label":"url"}],"paper_title":{"en":"Evaluation of inhibitory actions of flavonols and related substances on lysophospholipase d activity of serum autotaxin by a convenient assay using a chromogenic substrate.","ja":"Evaluation of inhibitory actions of flavonols and related substances on lysophospholipase d activity of serum autotaxin by a convenient assay using a chromogenic substrate."},"authors":{"en":[{"name":"Ueda Kaori"},{"name":"Yoshihara Masanori"},{"name":"Nakao Michiyasu"},{"name":"Tanaka Tamotsu"},{"name":"Sano Shigeki"},{"name":"Fukuzawa Kenji"},{"name":"Tokumura Akira"}],"ja":[{"name":"Ueda Kaori"},{"name":"Yoshihara Masanori"},{"name":"中尾 允泰"},{"name":"田中 保"},{"name":"佐野 茂樹"},{"name":"福澤 健治"},{"name":"德村 彰"}]},"description":{"en":"Overproduction of lysophosphatidic acid (LPA) by lysophospholipase D/autotaxin (lysoPLD/ATX) is postulated to be involved in the promotion of cancer and atherosclerosis. A lysoPLD inhibitor may be utilized to ameliorate the LPA-related pathological conditions. In this study, a new assay was devised to quantify p-nitrophenol from hydrolysis of chromogenic substrate by serum lysoPLD without tedious lipid extraction procedures. Flavonols, phenolic acids, free fatty acids, and N-acyltyrosines inhibited lysoPLD activity in a micromolar range. They were classified into competitive, noncompetitive, or mixed type inhibitors. The results show that the low hydrophobicity of an inhibitor is a critical factor in its preference for the binding to a noncatalytic binding site over a catalytic binding site. Considering its reported bioavailability and the low dependency of its inhibitory activity on serum dilution, flavonol is likely to be a more effective lysoPLD inhibitor in human blood circulation in vivo than the other inhibitors including LPA.","ja":"Overproduction of lysophosphatidic acid (LPA) by lysophospholipase D/autotaxin (lysoPLD/ATX) is postulated to be involved in the promotion of cancer and atherosclerosis. A lysoPLD inhibitor may be utilized to ameliorate the LPA-related pathological conditions. In this study, a new assay was devised to quantify p-nitrophenol from hydrolysis of chromogenic substrate by serum lysoPLD without tedious lipid extraction procedures. Flavonols, phenolic acids, free fatty acids, and N-acyltyrosines inhibited lysoPLD activity in a micromolar range. They were classified into competitive, noncompetitive, or mixed type inhibitors. The results show that the low hydrophobicity of an inhibitor is a critical factor in its preference for the binding to a noncatalytic binding site over a catalytic binding site. Considering its reported bioavailability and the low dependency of its inhibitory activity on serum dilution, flavonol is likely to be a more effective lysoPLD inhibitor in human blood circulation in vivo than the other inhibitors including LPA."},"publication_date":"2010-05-26","publication_name":{"en":"Journal of Agricultural and Food Chemistry","ja":"Journal of Agricultural and Food Chemistry"},"volume":"58","number":"10","starting_page":"6053","ending_page":"6063","languages":["eng"],"referee":true,"invited":true,"identifiers":{"doi":["10.1021/jf904155a"],"issn":["1520-5118"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/20213695","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=210619","label":"url"}],"paper_title":{"en":"A clean-up technology for the simultaneous determination of lysophosphatidic acid and sphingosine-1-phosphate by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using a phosphate-capture molecule, Phos-tag.","ja":"A clean-up technology for the simultaneous determination of lysophosphatidic acid and sphingosine-1-phosphate by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using a phosphate-capture molecule, Phos-tag."},"authors":{"en":[{"name":"Morishige Jun-ichi"},{"name":"Urikura Mai"},{"name":"Takagi Haruko"},{"name":"Hirano Kaoru"},{"name":"Koike Tohru"},{"name":"Tanaka Tamotsu"},{"name":"Satouchi Kiyoshi"}],"ja":[{"name":"Morishige Jun-ichi"},{"name":"Urikura Mai"},{"name":"Takagi Haruko"},{"name":"Hirano Kaoru"},{"name":"Koike Tohru"},{"name":"田中 保"},{"name":"Satouchi Kiyoshi"}]},"description":{"en":"Lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) are growth factor-like lipids having a phosphate group. The concentrations of these mediator lipids in blood are considered to be potential biomarkers for early detection of cancer or vascular diseases. Here, we report a method for simultaneous determination of LPA and S1P using Phos-tag, a zinc complex that specifically binds to a phosphate-monoester group. Although both LPA and S1P are hydrophilic compounds, we found that they acquire hydrophobic properties when they form complexes with Phos-tag. Based on this finding, we developed a method for the enrichment of LPA and S1P from biological samples. The first partition in a two-phase solvent system consisting of chloroform/methanol/water (1:1:0.9, v/v/v) is conducted for the removal of lipids. LPA and S1P are specifically extracted as Phos-tag complexes at the second partition by adding Phos-tag. The Phos-tag complexes of LPA and S1P are detectable by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and quantifiable based on the relative intensities of ions using 17:0 LPA and C17 S1P as internal standards. The protocol was validated by analyses of these mediator lipids in calf serum, a rat brain and a lung. The clean-up protocol is rapid, requires neither thin-layer chromatography (TLC) nor liquid chromatography (LC), and is applicable to both blood and solid tissue samples. We believe that our protocol will be useful for a routine analysis of LPA and S1P in many clinical samples.","ja":"Lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) are growth factor-like lipids having a phosphate group. The concentrations of these mediator lipids in blood are considered to be potential biomarkers for early detection of cancer or vascular diseases. Here, we report a method for simultaneous determination of LPA and S1P using Phos-tag, a zinc complex that specifically binds to a phosphate-monoester group. Although both LPA and S1P are hydrophilic compounds, we found that they acquire hydrophobic properties when they form complexes with Phos-tag. Based on this finding, we developed a method for the enrichment of LPA and S1P from biological samples. The first partition in a two-phase solvent system consisting of chloroform/methanol/water (1:1:0.9, v/v/v) is conducted for the removal of lipids. LPA and S1P are specifically extracted as Phos-tag complexes at the second partition by adding Phos-tag. The Phos-tag complexes of LPA and S1P are detectable by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) and quantifiable based on the relative intensities of ions using 17:0 LPA and C17 S1P as internal standards. The protocol was validated by analyses of these mediator lipids in calf serum, a rat brain and a lung. The clean-up protocol is rapid, requires neither thin-layer chromatography (TLC) nor liquid chromatography (LC), and is applicable to both blood and solid tissue samples. We believe that our protocol will be useful for a routine analysis of LPA and S1P in many clinical samples."},"publication_date":"2010-04-15","publication_name":{"en":"Rapid Communications in Mass Spectrometry: RCM","ja":"Rapid Communications in Mass Spectrometry: RCM"},"volume":"24","number":"7","starting_page":"1075","ending_page":"1084","languages":["eng"],"referee":true,"invited":true,"identifiers":{"doi":["10.1002/rcm.4484"],"issn":["1097-0231"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/19755413","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=210618","label":"url"}],"paper_title":{"en":"S1P3-mediated cardiac fibrosis in sphingosine kinase 1 transgenic mice involves reactive oxygen species.","ja":"S1P3-mediated cardiac fibrosis in sphingosine kinase 1 transgenic mice involves reactive oxygen species."},"authors":{"en":[{"name":"Takuwa Noriko"},{"name":"Ohkura Sei-Ichiro"},{"name":"Takashima Shin-Ichiro"},{"name":"Ohtani Keisuke"},{"name":"Okamoto Yasuo"},{"name":"Tanaka Tamotsu"},{"name":"Hirano Kaoru"},{"name":"Usui Soichiro"},{"name":"Wang Fei"},{"name":"Du Wa"},{"name":"Yoshioka Kazuaki"},{"name":"Banno Yoshiko"},{"name":"Sasaki Motoko"},{"name":"Ichi Ikuyo"},{"name":"Okamura Miwa"},{"name":"Sugimoto Naotoshi"},{"name":"Mizugishi Kiyomi"},{"name":"Nakanuma Yasuni"},{"name":"Ishii Isao"},{"name":"Takamura Masayuki"},{"name":"Kaneko Shuichi"},{"name":"Kojo Shosuke"},{"name":"Satouchi Kiyoshi"},{"name":"Mitumori Kunitoshi"},{"name":"Chun Jerold"},{"name":"Takuwa Yoh"}],"ja":[{"name":"Takuwa Noriko"},{"name":"Ohkura Sei-Ichiro"},{"name":"Takashima Shin-Ichiro"},{"name":"Ohtani Keisuke"},{"name":"Okamoto Yasuo"},{"name":"田中 保"},{"name":"Hirano Kaoru"},{"name":"Usui Soichiro"},{"name":"Wang Fei"},{"name":"Du Wa"},{"name":"Yoshioka Kazuaki"},{"name":"Banno Yoshiko"},{"name":"Sasaki Motoko"},{"name":"Ichi Ikuyo"},{"name":"Okamura Miwa"},{"name":"Sugimoto Naotoshi"},{"name":"Mizugishi Kiyomi"},{"name":"Nakanuma Yasuni"},{"name":"Ishii Isao"},{"name":"Takamura Masayuki"},{"name":"Kaneko Shuichi"},{"name":"Kojo Shosuke"},{"name":"Satouchi Kiyoshi"},{"name":"Mitumori Kunitoshi"},{"name":"Chun Jerold"},{"name":"Takuwa Yoh"}]},"description":{"en":"AIMS: Sphingosine kinase 1 (SPHK1), its product sphingosine-1-phosphate (S1P), and S1P receptor subtypes have been suggested to play protective roles for cardiomyocytes in animal models of ischaemic preconditioning and cardiac ischaemia/reperfusion injury. To get more insight into roles for SPHK1 in vivo, we have generated SPHK1-transgenic (TG) mice and analysed the cardiac phenotype. METHODS AND RESULTS: SPHK1-TG mice overexpressed SPHK1 in diverse tissues, with a nearly 20-fold increase in enzymatic activity. The TG mice grew normally with normal blood chemistry, cell counts, heart rate, and blood pressure. Unexpectedly, TG mice with high but not low expression levels of SPHK1 developed progressive myocardial degeneration and fibrosis, with upregulation of embryonic genes, elevated RhoA and Rac1 activity, stimulation of Smad3 phosphorylation, and increased levels of oxidative stress markers. Treatment of juvenile TG mice with pitavastatin, an established inhibitor of the Rho family G proteins, or deletion of S1P3, a major myocardial S1P receptor subtype that couples to Rho GTPases and transactivates Smad signalling, both inhibited cardiac fibrosis with concomitant inhibition of SPHK1-dependent Smad-3 phosphorylation. In addition, the anti-oxidant N-2-mercaptopropyonylglycine, which reduces reactive oxygen species (ROS), also inhibited cardiac fibrosis. In in vivo ischaemia/reperfusion injury, the size of myocardial infarct was 30% decreased in SPHK1-TG mice compared with wild-type mice. CONCLUSION: These results suggest that chronic activation of SPHK1-S1P signalling results in both pathological cardiac remodelling through ROS mediated by S1P3 and favourable cardioprotective effects.","ja":"AIMS: Sphingosine kinase 1 (SPHK1), its product sphingosine-1-phosphate (S1P), and S1P receptor subtypes have been suggested to play protective roles for cardiomyocytes in animal models of ischaemic preconditioning and cardiac ischaemia/reperfusion injury. To get more insight into roles for SPHK1 in vivo, we have generated SPHK1-transgenic (TG) mice and analysed the cardiac phenotype. METHODS AND RESULTS: SPHK1-TG mice overexpressed SPHK1 in diverse tissues, with a nearly 20-fold increase in enzymatic activity. The TG mice grew normally with normal blood chemistry, cell counts, heart rate, and blood pressure. Unexpectedly, TG mice with high but not low expression levels of SPHK1 developed progressive myocardial degeneration and fibrosis, with upregulation of embryonic genes, elevated RhoA and Rac1 activity, stimulation of Smad3 phosphorylation, and increased levels of oxidative stress markers. Treatment of juvenile TG mice with pitavastatin, an established inhibitor of the Rho family G proteins, or deletion of S1P3, a major myocardial S1P receptor subtype that couples to Rho GTPases and transactivates Smad signalling, both inhibited cardiac fibrosis with concomitant inhibition of SPHK1-dependent Smad-3 phosphorylation. In addition, the anti-oxidant N-2-mercaptopropyonylglycine, which reduces reactive oxygen species (ROS), also inhibited cardiac fibrosis. In in vivo ischaemia/reperfusion injury, the size of myocardial infarct was 30% decreased in SPHK1-TG mice compared with wild-type mice. CONCLUSION: These results suggest that chronic activation of SPHK1-S1P signalling results in both pathological cardiac remodelling through ROS mediated by S1P3 and favourable cardioprotective effects."},"publication_date":"2009-09-15","publication_name":{"en":"Cardiovascular Research","ja":"Cardiovascular Research"},"volume":"85","number":"3","starting_page":"484","ending_page":"493","languages":["eng"],"referee":true,"invited":true,"identifiers":{"doi":["10.1093/cvr/cvp312"],"issn":["1755-3245"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/10027542114/","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/19502739","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390282681457031808/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=210617","label":"url"}],"paper_title":{"en":"Formation of lysophosphatidic acid, a wound-healing lipid, during digestion of cabbage leaves.","ja":"Formation of lysophosphatidic acid, a wound-healing lipid, during digestion of cabbage leaves."},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Horiuchi Gou"},{"name":"Matsuoka Megumi"},{"name":"Hirano Kaoru"},{"name":"Tokumura Akira"},{"name":"Koike Tohru"},{"name":"Satouchi Kiyoshi"}],"ja":[{"name":"田中 保"},{"name":"Horiuchi Gou"},{"name":"Matsuoka Megumi"},{"name":"Hirano Kaoru"},{"name":"Tokumura Akira"},{"name":"Koike Tohru"},{"name":"Satouchi Kiyoshi"}]},"description":{"en":"Lysophosphatidic acid (LPA) is a lipid mediator that plays a role in the process of wound healing in animal tissues, including the digestive tract. We determined LPA in several foodstuffs, and found that cabbage leaves were the richest source of LPA. We also found that, at 22 and 195 nmol/g (wet weight), LPA and phosphatidic acid (PA) were respectively formed during mastication of raw cabbage leaves and that the resulting PA was converted to LPA by pancreatic phospholipase A(2). The lipid extract obtained from ground cabbage leaves promoted the proliferation of Swiss 3T3 fibroblasts and the motility of HGC-27 cells, stomach-derived epithelial-like cells, at physiologically relevant concentrations. These activities of cabbage lipids were inhibited by Ki16425, an LPA-receptor antagonist. LPA formed during the digestion of cabbage leaves may be one of the components in the beneficial effect of ingested cabbage on a damaged digestive tract.","ja":"Lysophosphatidic acid (LPA) is a lipid mediator that plays a role in the process of wound healing in animal tissues, including the digestive tract. We determined LPA in several foodstuffs, and found that cabbage leaves were the richest source of LPA. We also found that, at 22 and 195 nmol/g (wet weight), LPA and phosphatidic acid (PA) were respectively formed during mastication of raw cabbage leaves and that the resulting PA was converted to LPA by pancreatic phospholipase A(2). The lipid extract obtained from ground cabbage leaves promoted the proliferation of Swiss 3T3 fibroblasts and the motility of HGC-27 cells, stomach-derived epithelial-like cells, at physiologically relevant concentrations. These activities of cabbage lipids were inhibited by Ki16425, an LPA-receptor antagonist. LPA formed during the digestion of cabbage leaves may be one of the components in the beneficial effect of ingested cabbage on a damaged digestive tract."},"publication_date":"2009-06-07","publication_name":{"en":"Bioscience, Biotechnology, and Biochemistry","ja":"Bioscience, Biotechnology, and Biochemistry"},"volume":"73","number":"6","starting_page":"1293","ending_page":"1300","languages":["eng"],"referee":true,"invited":true,"identifiers":{"doi":["10.1271/bbb.80813"],"issn":["1347-6947"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/18758077","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=190208","label":"url"}],"paper_title":{"en":"Inhibitory effect of juniperonic acid (Delta-5c,11c,14c,17c-20:4, omega-3) on bombesin-induced proliferation of Swiss 3T3 cells.","ja":"Inhibitory effect of juniperonic acid (Delta-5c,11c,14c,17c-20:4, omega-3) on bombesin-induced proliferation of Swiss 3T3 cells."},"authors":{"en":[{"name":"Morishige Jun-ichi"},{"name":"Amano Naoki"},{"name":"Hirano Kaoru"},{"name":"Nishio Hiroaki"},{"name":"Tanaka Tamotsu"},{"name":"Satouchi Kiyoshi"}],"ja":[{"name":"Morishige Jun-ichi"},{"name":"Amano Naoki"},{"name":"Hirano Kaoru"},{"name":"Nishio Hiroaki"},{"name":"田中 保"},{"name":"Satouchi Kiyoshi"}]},"description":{"en":"Juniperonic acid (Delta-5c,11c,14c,17c-20:4, JA) is a polymethylene-interrupted (PMI) fatty acid that occurs in Biota orientalis. In this study, we found that JA has an antiproliferative activity. Swiss 3T3 cells were preloaded with fatty acids before stimulation with bombesin, a mitogenic neuropeptide, and proliferation of the cells was assessed by [(3)H]thymidine incorporation. Preloading of linoleic acid (Delta-9c,12c-18:2) significantly enhanced bombesin-induced proliferation. In contrast, preloading of eicosapentaenoic acid (Delta-5c,8c,11c,14c,17c-20:5, EPA) suppressed proliferation. Likewise, cells preloaded with JA showed a significantly curtailed response to bombesin. The antiproliferative potency of JA was equivalent to that of EPA. Sciadonic acid (Delta-5c,11c,14c-20:3), an omega-6 analogue of JA did not show antiproliferative activity, suggesting the importance of the omega-3 double bond rather than the PMI structure. The EPA-like activity of JA may be involved in the pharmaceutical activity of biota seeds, a psychoactive Chinese traditional medicine.","ja":"Juniperonic acid (Delta-5c,11c,14c,17c-20:4, JA) is a polymethylene-interrupted (PMI) fatty acid that occurs in Biota orientalis. In this study, we found that JA has an antiproliferative activity. Swiss 3T3 cells were preloaded with fatty acids before stimulation with bombesin, a mitogenic neuropeptide, and proliferation of the cells was assessed by [(3)H]thymidine incorporation. Preloading of linoleic acid (Delta-9c,12c-18:2) significantly enhanced bombesin-induced proliferation. In contrast, preloading of eicosapentaenoic acid (Delta-5c,8c,11c,14c,17c-20:5, EPA) suppressed proliferation. Likewise, cells preloaded with JA showed a significantly curtailed response to bombesin. The antiproliferative potency of JA was equivalent to that of EPA. Sciadonic acid (Delta-5c,11c,14c-20:3), an omega-6 analogue of JA did not show antiproliferative activity, suggesting the importance of the omega-3 double bond rather than the PMI structure. The EPA-like activity of JA may be involved in the pharmaceutical activity of biota seeds, a psychoactive Chinese traditional medicine."},"publication_date":"2008-09","publication_name":{"en":"Biological & Pharmaceutical Bulletin","ja":"Biological & Pharmaceutical Bulletin"},"volume":"31","number":"9","starting_page":"1786","ending_page":"1789","languages":["eng"],"referee":true,"invited":true,"identifiers":{"doi":["10.1248/bpb.31.1786"],"issn":["0918-6158"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/17451430","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177266","label":"url"}],"paper_title":{"en":"Metabolic pathway that produces essential fatty acids from polymethylene-interrupted polyunsaturated fatty acids in animal cells","ja":"Metabolic pathway that produces essential fatty acids from polymethylene-interrupted polyunsaturated fatty acids in animal cells"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Morishige J."},{"name":"Iwawaki D."},{"name":"Fukuhara T."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Morishige J."},{"name":"Iwawaki D."},{"name":"Fukuhara T."},{"name":"Satouchi K."}]},"description":{"en":"Sciadonic acid (20:3 Delta-5,11,14) and juniperonic acid (20:4 Delta-5,11,14,17) are polyunsaturated fatty acids (PUFAs) that lack the Delta-8 double bond of arachidonic acid (20:4 Delta-5,8,11,14) and eicosapentaenoic acid (20:5 Delta-5,8,11,14,17), respectively. Here, we demonstrate that these conifer oil-derived PUFAs are metabolized to essential fatty acids in animal cells. When Swiss 3T3 cells were cultured with sciadonic acid, linoleic acid (18:2 Delta-9,12) accumulated in the cells to an extent dependent on the concentration of sciadonic acid. At the same time, a small amount of 16:2 Delta-7,10 appeared in the cellular lipids. Both 16:2 Delta-7,10 and linoleic acid accumulated in sciadonic acid-supplemented CHO cells, but not in peroxisome-deficient CHO cells. We confirmed that 16:2 Delta-7,10 was effectively elongated to linoleic acid in rat liver microsomes. These results indicate that sciadonic acid was partially degraded to 16:2 Delta-7,10 by two cycles of beta-oxidation in peroxisomes, then elongated to linoleic acid in microsomes. Supplementation of Swiss 3T3 cells with juniperonic acid, an n-3 analogue of sciadonic acid, induced accumulation of alpha-linolenic acid (18:3 Delta-9,12,15) in cellular lipids, suggesting that juniperonic acid was metabolized in a similar manner to sciadonic acid. This PUFA remodeling is thought to be a process that converts unsuitable fatty acids into essential fatty acids required by animals.","ja":"Sciadonic acid (20:3 Delta-5,11,14) and juniperonic acid (20:4 Delta-5,11,14,17) are polyunsaturated fatty acids (PUFAs) that lack the Delta-8 double bond of arachidonic acid (20:4 Delta-5,8,11,14) and eicosapentaenoic acid (20:5 Delta-5,8,11,14,17), respectively. Here, we demonstrate that these conifer oil-derived PUFAs are metabolized to essential fatty acids in animal cells. When Swiss 3T3 cells were cultured with sciadonic acid, linoleic acid (18:2 Delta-9,12) accumulated in the cells to an extent dependent on the concentration of sciadonic acid. At the same time, a small amount of 16:2 Delta-7,10 appeared in the cellular lipids. Both 16:2 Delta-7,10 and linoleic acid accumulated in sciadonic acid-supplemented CHO cells, but not in peroxisome-deficient CHO cells. We confirmed that 16:2 Delta-7,10 was effectively elongated to linoleic acid in rat liver microsomes. These results indicate that sciadonic acid was partially degraded to 16:2 Delta-7,10 by two cycles of beta-oxidation in peroxisomes, then elongated to linoleic acid in microsomes. Supplementation of Swiss 3T3 cells with juniperonic acid, an n-3 analogue of sciadonic acid, induced accumulation of alpha-linolenic acid (18:3 Delta-9,12,15) in cellular lipids, suggesting that juniperonic acid was metabolized in a similar manner to sciadonic acid. This PUFA remodeling is thought to be a process that converts unsuitable fatty acids into essential fatty acids required by animals."},"publication_date":"2007-04-20","publication_name":{"en":"The FEBS Journal","ja":"The FEBS Journal"},"volume":"274","number":"11","starting_page":"2728","ending_page":"2737","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1111/j.1742-4658.2007.05807.x"],"issn":["1742-464X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/17308334","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177259","label":"url"}],"paper_title":{"en":"CGI-58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation","ja":"CGI-58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation"},"authors":{"en":[{"name":"Yamaguchi T."},{"name":"Omatsu N."},{"name":"Morimoto E."},{"name":"Nakashima H."},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Yamaguchi T."},{"name":"Omatsu N."},{"name":"Morimoto E."},{"name":"Nakashima H."},{"name":"田中 保"}]},"description":{"en":"A lipid droplet (LD)-associated protein, perilipin, is a critical regulator of lipolysis in adipocytes. We previously showed that Comparative Gene Identification-58 (CGI-58), a product of the causal gene of Chanarin-Dorfman syndrome, interacts with perilipin on LDs. In this study, we investigated the function of CGI-58 using RNA interference. Notably, CGI-58 knockdown caused an abnormal accumulation of LDs in both 3T3-L1 preadipocytes and Hepa1 hepatoma cells. CGI-58 knockdown did not influence the differentiation of 3T3-L1 adipocytes but reduced the activity of both basal and cAMP-dependent protein kinase-stimulated lipolysis. In vitro studies showed that CGI-58 itself does not have lipase/esterase activity, but it enhanced the activity of adipose triglyceride lipase. Upon lipolytic stimulation, endogenous CGI-58 was rapidly dispersed from LDs into the cytosol along with small particulate structures. This shift in localization depends on the phosphorylation of perilipin, because phosphorylated perilipin lost the ability to bind CGI-58. During lipolytic activation, LDs in adipocytes vesiculate into micro-LDs. Using coherent anti-Stokes Raman scattering microscopy, we pursued the formation of micro-LDs in single cells, which seemed to occur in cytoplasmic regions distant from the large central LDs. CGI-58 is not required for this process. Thus, CGI-58 facilitates lipolysis in cooperation with perilipin and other factors, including lipases.","ja":"A lipid droplet (LD)-associated protein, perilipin, is a critical regulator of lipolysis in adipocytes. We previously showed that Comparative Gene Identification-58 (CGI-58), a product of the causal gene of Chanarin-Dorfman syndrome, interacts with perilipin on LDs. In this study, we investigated the function of CGI-58 using RNA interference. Notably, CGI-58 knockdown caused an abnormal accumulation of LDs in both 3T3-L1 preadipocytes and Hepa1 hepatoma cells. CGI-58 knockdown did not influence the differentiation of 3T3-L1 adipocytes but reduced the activity of both basal and cAMP-dependent protein kinase-stimulated lipolysis. In vitro studies showed that CGI-58 itself does not have lipase/esterase activity, but it enhanced the activity of adipose triglyceride lipase. Upon lipolytic stimulation, endogenous CGI-58 was rapidly dispersed from LDs into the cytosol along with small particulate structures. This shift in localization depends on the phosphorylation of perilipin, because phosphorylated perilipin lost the ability to bind CGI-58. During lipolytic activation, LDs in adipocytes vesiculate into micro-LDs. Using coherent anti-Stokes Raman scattering microscopy, we pursued the formation of micro-LDs in single cells, which seemed to occur in cytoplasmic regions distant from the large central LDs. CGI-58 is not required for this process. Thus, CGI-58 facilitates lipolysis in cooperation with perilipin and other factors, including lipases."},"publication_date":"2007-02-17","publication_name":{"en":"Journal of Lipid Research","ja":"Journal of Lipid Research"},"volume":"48","number":"5","starting_page":"1078","ending_page":"1089","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1194/jlr.M600493-JLR200"],"issn":["0022-2275"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/17321793","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=163551","label":"url"}],"paper_title":{"en":"Production of bioactive lysophosphatidic acid by lysophospholipase D in hen egg white","ja":"Production of bioactive lysophosphatidic acid by lysophospholipase D in hen egg white"},"authors":{"en":[{"name":"Morishige Junichi"},{"name":"Touchika Kanako"},{"name":"Tanaka Tamotsu"},{"name":"Satouchi Kiyoshi"},{"name":"Fukuzawa Kenji"},{"name":"Tokumura Akira"}],"ja":[{"name":"Morishige Junichi"},{"name":"Touchika Kanako"},{"name":"田中 保"},{"name":"Satouchi Kiyoshi"},{"name":"福澤 健治"},{"name":"德村 彰"}]},"description":{"en":"Lysophosphatidic acid (LPA), a lysophospholipid mediator, is produced extracellularly by lysophospholipase D (lysoPLD) secreted in several animal body fluids including blood plasma. Previously, we reported that hen egg white contains polyunsaturated fatty acid-rich LPA. In this study, we examined whether lysoPLD is involved in the production of LPA in hen egg white. LysoPLD activity was measured by determining LPA and choline by mass spectrometric and enzyme-linked fluorometric analyses, respectively. LysoPLD increased with increased dilution of egg white, indicating that one or more components of egg white strongly inhibit its lysoPLD activity. This dilution-dependent increase in the lysoPLD activity was masked by co-incubation of the egg white with lysozyme, a major protein in hen egg white. Furthermore, addition of Zn(2+), Mn(2+), Ni(2+), or Co(2+) to diluted egg white altered preference patterns of lysoPLD toward choline-containing substrates. In particular, the egg white lysoPLD activity was greatly increased when Co(2+) was added. The cation-requirement of lysoPLD activity in hen egg white resembled that of plasma autotaxin (ATX)/lysoPLD. Western blot analysis revealed that egg white contained a protein that was immunostained with anti-ATX antibody. These results suggested that LPA in hen egg white is produced from lysophospholipids, especially LPC, by the action of ATX/lysoPLD, possibly originating from hen oviduct fluid.","ja":"Lysophosphatidic acid (LPA), a lysophospholipid mediator, is produced extracellularly by lysophospholipase D (lysoPLD) secreted in several animal body fluids including blood plasma. Previously, we reported that hen egg white contains polyunsaturated fatty acid-rich LPA. In this study, we examined whether lysoPLD is involved in the production of LPA in hen egg white. LysoPLD activity was measured by determining LPA and choline by mass spectrometric and enzyme-linked fluorometric analyses, respectively. LysoPLD increased with increased dilution of egg white, indicating that one or more components of egg white strongly inhibit its lysoPLD activity. This dilution-dependent increase in the lysoPLD activity was masked by co-incubation of the egg white with lysozyme, a major protein in hen egg white. Furthermore, addition of Zn(2+), Mn(2+), Ni(2+), or Co(2+) to diluted egg white altered preference patterns of lysoPLD toward choline-containing substrates. In particular, the egg white lysoPLD activity was greatly increased when Co(2+) was added. The cation-requirement of lysoPLD activity in hen egg white resembled that of plasma autotaxin (ATX)/lysoPLD. Western blot analysis revealed that egg white contained a protein that was immunostained with anti-ATX antibody. These results suggested that LPA in hen egg white is produced from lysophospholipids, especially LPC, by the action of ATX/lysoPLD, possibly originating from hen oviduct fluid."},"publication_date":"2007-01-19","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids","ja":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"},"volume":"1771","number":"4","starting_page":"491","ending_page":"499","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbalip.2007.01.005"],"issn":["1388-1981"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/16417288","label":"url"},{"@id":"https://www.scopus.com/pages/publications/33644501134","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177256","label":"url"}],"paper_title":{"en":"Lupane-type saponins from leaves of Acanthopanax sessiliflorus and their inhibitory activity on pancreatic lipase","ja":"Lupane-type saponins from leaves of Acanthopanax sessiliflorus and their inhibitory activity on pancreatic lipase"},"authors":{"en":[{"name":"Yoshizumi Kazuma"},{"name":"Hirano Kaoru"},{"name":"Ando Hidehiro"},{"name":"Tanaka Tamotsu"},{"name":"Terao Junji"}],"ja":[{"name":"Yoshizumi Kazuma"},{"name":"Hirano Kaoru"},{"name":"Ando Hidehiro"},{"name":"田中 保"},{"name":"Terao Junji"}]},"description":{"en":"Three known saponins, chiisanoside, 11-deoxyisochiisanoside, and isochiisanoside, and one novel saponin, 3,4-seco-4(23),20(29)-lupadiene-3,28-dioic acid 28-O-alpha-l-rhamnopyranosyl (1-->4)-beta-d-glucopyranosyl (1-->6)-beta-d-glucopyranoside, referred to as sessiloside, were isolated from a hot water extract of Acanthopanax sessiliflorus leaves. All of these saponins were lupane-type triterpene triglycosides, and their concentrations were 4.1, 1.0, 0.5, and 0.4% (w/w) of the total extract, respectively. Sessiloside and chiisanoside inhibited pancreatic lipase activity in vitro, and addition of the saponin-rich fraction to a high-fat diet suppressed the body weight gain of mice. The possibility of application of the lupane-type saponins from A. sessiliflorus leaves to the treatment of obesity is discussed.","ja":"Three known saponins, chiisanoside, 11-deoxyisochiisanoside, and isochiisanoside, and one novel saponin, 3,4-seco-4(23),20(29)-lupadiene-3,28-dioic acid 28-O-alpha-l-rhamnopyranosyl (1-->4)-beta-d-glucopyranosyl (1-->6)-beta-d-glucopyranoside, referred to as sessiloside, were isolated from a hot water extract of Acanthopanax sessiliflorus leaves. All of these saponins were lupane-type triterpene triglycosides, and their concentrations were 4.1, 1.0, 0.5, and 0.4% (w/w) of the total extract, respectively. Sessiloside and chiisanoside inhibited pancreatic lipase activity in vitro, and addition of the saponin-rich fraction to a high-fat diet suppressed the body weight gain of mice. The possibility of application of the lupane-type saponins from A. sessiliflorus leaves to the treatment of obesity is discussed."},"publication_date":"2006-01-25","publication_name":{"en":"Journal of Agricultural and Food Chemistry","ja":"Journal of Agricultural and Food Chemistry"},"volume":"54","number":"2","starting_page":"335","ending_page":"341","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1021/jf052047f"],"issn":["0021-8561"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15884763","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177252","label":"url"}],"paper_title":{"en":"Production and protein kinase C activation of diacylglycerols with polymethylene-interrupted PUFA residues","ja":"Production and protein kinase C activation of diacylglycerols with polymethylene-interrupted PUFA residues"},"authors":{"en":[{"name":"Morishige J."},{"name":"Takai Y."},{"name":"Hirano K."},{"name":"Tanaka Tamotsu"},{"name":"Satouchi K."}],"ja":[{"name":"Morishige J."},{"name":"Takai Y."},{"name":"Hirano K."},{"name":"田中 保"},{"name":"Satouchi K."}]},"description":{"en":"Sciadonic acid (20:3, delta-5c,11 c,14c) is a polymethylene-interrupted PUFA (PMI-PUFA) that is present in conifer seeds and known to be incorporated into animal cells and to accumulate in membrane PI as a substitute for arachidonate. In this study, we investigated whether PI having sciadonate could serve as source of DAG that could activate protein kinase C (PKC). When Swiss 3T3 cells cultured with sciadonic acid were stimulated with 100 nM of bombesin, 1-stearoyl-2-sciadonoyl-glycerol (G) and 1-stearoyl-2-arachidonoyl-G were produced. The net increments of these two molecular species of DAG reflected the levels of the two molecular species in the PI in the cells. When cells cultured with juniperonic acid (20:4, delta-5c,11c,14c,17c) were stimulated, 1-stearoyl-2-juniperonoyl-G was produced in proportion to the level of this molecular species in PI in the cells. We also examined PKC activation by synthetic DAG using a partially purified PKC fraction from rat brain and found that both 1-stearoyl-2-sciadonoyl-G and 1-stearoyl-2-juniperonoyl-G could activate PKC comparably to 1 -stearoyl-2-arachidonoyl-G. These results indicate that 1-stearoyl-PI having these C20 PMI-PUFA residues can serve as sources of potential signaling molecules.","ja":"Sciadonic acid (20:3, delta-5c,11 c,14c) is a polymethylene-interrupted PUFA (PMI-PUFA) that is present in conifer seeds and known to be incorporated into animal cells and to accumulate in membrane PI as a substitute for arachidonate. In this study, we investigated whether PI having sciadonate could serve as source of DAG that could activate protein kinase C (PKC). When Swiss 3T3 cells cultured with sciadonic acid were stimulated with 100 nM of bombesin, 1-stearoyl-2-sciadonoyl-glycerol (G) and 1-stearoyl-2-arachidonoyl-G were produced. The net increments of these two molecular species of DAG reflected the levels of the two molecular species in the PI in the cells. When cells cultured with juniperonic acid (20:4, delta-5c,11c,14c,17c) were stimulated, 1-stearoyl-2-juniperonoyl-G was produced in proportion to the level of this molecular species in PI in the cells. We also examined PKC activation by synthetic DAG using a partially purified PKC fraction from rat brain and found that both 1-stearoyl-2-sciadonoyl-G and 1-stearoyl-2-juniperonoyl-G could activate PKC comparably to 1 -stearoyl-2-arachidonoyl-G. These results indicate that 1-stearoyl-PI having these C20 PMI-PUFA residues can serve as sources of potential signaling molecules."},"publication_date":"2005-02","publication_name":{"en":"Lipids","ja":"Lipids"},"volume":"40","number":"2","starting_page":"155","ending_page":"162","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s11745-005-1370-8"],"issn":["0024-4201"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"http://www.jlr.org/cgi/content/full/45/11/2145","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15314093","label":"url"},{"@id":"https://www.scopus.com/pages/publications/17144406220","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=145926","label":"url"}],"paper_title":{"en":"Quantitative analysis of lysophosphatidic acid by time-of-flight mass spectrometry using a phosphate-capture molecule","ja":"Quantitative analysis of lysophosphatidic acid by time-of-flight mass spectrometry using a phosphate-capture molecule"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Tsutsui Hideki"},{"name":"Hirano Kaoru"},{"name":"Koike Tohru"},{"name":"Tokumura Akira"},{"name":"Satouchi Kiyoshi"}],"ja":[{"name":"田中 保"},{"name":"Tsutsui Hideki"},{"name":"Hirano Kaoru"},{"name":"Koike Tohru"},{"name":"德村 彰"},{"name":"Satouchi Kiyoshi"}]},"description":{"en":"Lysophosphatidic acid (LPA) is a lipid mediator that may play an important role in wound healing, embryonic development, and progression of cancer. Here, we report a procedure for the quantification of LPA by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The method is based on a characteristic mass shift with total charge change (from -2 to +1) of the phosphate species due to 1:1 complexation of LPA(2-) with a dinuclear zinc (II) complex [1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-olato dizinc(II) complex; Zn(2)L(3+)] at physiological pH. The monocationic complex [LPA(2-)-Zn(2)L(3+)](+) was detected in the positive mode, in which no other signal of cation adducts of LPA(2-) was observed. The detection limit of 18:1 LPA by this method was 0.1 pmol on a sample plate. The intensity ratio of [LPA(2-)-Zn(2)L(3+)](+) against an internal standard [17:0 LPA(2-)-Zn(2)L(3+)](+) increased linearly with their molar ratio. Based on the relative intensities of complex ions, we determined the amounts of LPA homologs in an egg white by this method; the results obtained were in good agreement with those by gas liquid chromatography. This sensitive and convenient procedure for LPA-specific detection is useful for the quantification of LPA homologs occurring in biological materials.","ja":"Lysophosphatidic acid (LPA) is a lipid mediator that may play an important role in wound healing, embryonic development, and progression of cancer. Here, we report a procedure for the quantification of LPA by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The method is based on a characteristic mass shift with total charge change (from -2 to +1) of the phosphate species due to 1:1 complexation of LPA(2-) with a dinuclear zinc (II) complex [1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-olato dizinc(II) complex; Zn(2)L(3+)] at physiological pH. The monocationic complex [LPA(2-)-Zn(2)L(3+)](+) was detected in the positive mode, in which no other signal of cation adducts of LPA(2-) was observed. The detection limit of 18:1 LPA by this method was 0.1 pmol on a sample plate. The intensity ratio of [LPA(2-)-Zn(2)L(3+)](+) against an internal standard [17:0 LPA(2-)-Zn(2)L(3+)](+) increased linearly with their molar ratio. Based on the relative intensities of complex ions, we determined the amounts of LPA homologs in an egg white by this method; the results obtained were in good agreement with those by gas liquid chromatography. This sensitive and convenient procedure for LPA-specific detection is useful for the quantification of LPA homologs occurring in biological materials."},"publication_date":"2004-11","publication_name":{"en":"Journal of Lipid Research","ja":"Journal of Lipid Research"},"volume":"45","number":"11","starting_page":"2145","ending_page":"2150","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1194/jlr.D400010-JLR200"],"issn":["0022-2275"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15625317","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177247","label":"url"}],"paper_title":{"en":"Production of 1,2-didocosahexaenoyl phosphatidylcholine by bonito muscle lysophosphatidylcholine/transacylase","ja":"Production of 1,2-didocosahexaenoyl phosphatidylcholine by bonito muscle lysophosphatidylcholine/transacylase"},"authors":{"en":[{"name":"Hirano K."},{"name":"Matsui H."},{"name":"Tanaka Tamotsu"},{"name":"Matsuura F."},{"name":"Satouchi K."}],"ja":[{"name":"Hirano K."},{"name":"Matsui H."},{"name":"田中 保"},{"name":"Matsuura F."},{"name":"Satouchi K."}]},"description":{"en":"1,2-Didocosahexaenoyl phosphatidylcholine (PC), which has highly unsaturated fatty acid at both sn-1 and sn-2 positions of glycerol, is a characteristic molecular species of bonito muscle. To examine the involvement of a de novo route in its synthesis, the molecular species of phosphatidic acid (PA) were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using a 1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-olato dizinc(II) complex, a novel phosphate-capture molecule. However, 1,2-didocosahexaenoyl species could not be detected. Next, 1,2-didocosahexaenoyl PC synthesis by the cytosolic lysophosphatidylcholine (LPC)/transacylase was examined using endogenous LPC from bonito muscle, in which the 2-docosahexaenoyl species is abundant. The LPC/transacylase synthesized 1,2-didocosahexaenoyl PC as the most abundant molecular species. For further characterization, the LPC/transacylase was purified to homogeneity from the 100,000 x g supernatant of bonito muscle. The isolated LPC/transacylase is a labile glycoprotein with molecular mass of 52 kDa including a 5-kDa sugar moiety. The LPC/transacylase showed a PC synthesis (transacylase activity) below and above the critical micelle concentration of substrate LPC, and fatty acid release (lysophospholipase activity) was always smaller than the transacylase activity, even with a monomeric substrate. These results suggest that the LPC/transacylase is responsible for the synthesis of 1,2-didocosahexaenoyl PC.","ja":"1,2-Didocosahexaenoyl phosphatidylcholine (PC), which has highly unsaturated fatty acid at both sn-1 and sn-2 positions of glycerol, is a characteristic molecular species of bonito muscle. To examine the involvement of a de novo route in its synthesis, the molecular species of phosphatidic acid (PA) were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using a 1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-olato dizinc(II) complex, a novel phosphate-capture molecule. However, 1,2-didocosahexaenoyl species could not be detected. Next, 1,2-didocosahexaenoyl PC synthesis by the cytosolic lysophosphatidylcholine (LPC)/transacylase was examined using endogenous LPC from bonito muscle, in which the 2-docosahexaenoyl species is abundant. The LPC/transacylase synthesized 1,2-didocosahexaenoyl PC as the most abundant molecular species. For further characterization, the LPC/transacylase was purified to homogeneity from the 100,000 x g supernatant of bonito muscle. The isolated LPC/transacylase is a labile glycoprotein with molecular mass of 52 kDa including a 5-kDa sugar moiety. The LPC/transacylase showed a PC synthesis (transacylase activity) below and above the critical micelle concentration of substrate LPC, and fatty acid release (lysophospholipase activity) was always smaller than the transacylase activity, even with a monomeric substrate. These results suggest that the LPC/transacylase is responsible for the synthesis of 1,2-didocosahexaenoyl PC."},"publication_date":"2004-10","publication_name":{"en":"The Journal of Biochemistry","ja":"The Journal of Biochemistry"},"volume":"136","number":"4","starting_page":"477","ending_page":"483","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1093/jb/mvh145"],"issn":["0021-924X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/12654002","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177239","label":"url"}],"paper_title":{"en":"Mechanisms of accumulation of arachidonate in phosphatidylinositol in yellowtail: A comparative study of acylation systems of phospholipids in rat","ja":"Mechanisms of accumulation of arachidonate in phosphatidylinositol in yellowtail: A comparative study of acylation systems of phospholipids in rat"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Iwawaki D."},{"name":"Sakamoto M."},{"name":"Takai Y."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Iwawaki D."},{"name":"Sakamoto M."},{"name":"Takai Y."},{"name":"Satouchi K."}]},"description":{"en":"It is known that phosphatidylinositol (PtdIns) contains abundant arachidonate and is composed mainly of 1-stearoyl-2-arachidonoyl species in mammals. We investigated if this characteristic of PtdIns applies to the PtdIns from yellowtail (Seriola quinqueradiata), a marine fish. In common with phosphatidylcholine (PtdCho), phosphatidylethanolamine (PtdEtn) and phosphatidylserine (PtdSer) from brain, heart, liver, spleen, kidney and ovary, the predominant polyunsaturated fatty acid was docosahexaenoic acid, and levels of arachidonic acid were less than 4.5% (PtdCho), 7.5% (PtdEtn) and 3.0% (PtdSer) in these tissues. In striking contrast, arachidonic acid made up 17.6%, 31.8%, 27.8%, 26.1%, 25.4% and 33.5% of the fatty acid composition of PtdIns from brain, heart, liver, spleen, kidney and ovary, respectively. The most abundant molecular species of PtdIns in all these tissues was 1-stearoyl-2-arachidonoyl. Assay of acyltransferase in liver microsomes of yellowtail showed that arachidonic acid was incorporated into PtdIns more effectively than docosahexaenoic acid and that the latter inhibited incorporation of arachidonic acid into PtdCho without inhibiting the utilization of arachidonic acid for PtdIns. This effect of docosahexaenoic acid was not observed in similar experiments using rat liver microsomes and is thought to contribute to the exclusive utilization of arachidonic acid for acylation to PtdIns in yellowtail. Inositolphospholipids and their hydrolysates are known to act as signaling molecules in cells. The conserved hydrophobic structure of PtdIns (the 1-stearoyl-2-arachidonoyl moiety) may have physiological significance not only in mammals but also in fish.","ja":"It is known that phosphatidylinositol (PtdIns) contains abundant arachidonate and is composed mainly of 1-stearoyl-2-arachidonoyl species in mammals. We investigated if this characteristic of PtdIns applies to the PtdIns from yellowtail (Seriola quinqueradiata), a marine fish. In common with phosphatidylcholine (PtdCho), phosphatidylethanolamine (PtdEtn) and phosphatidylserine (PtdSer) from brain, heart, liver, spleen, kidney and ovary, the predominant polyunsaturated fatty acid was docosahexaenoic acid, and levels of arachidonic acid were less than 4.5% (PtdCho), 7.5% (PtdEtn) and 3.0% (PtdSer) in these tissues. In striking contrast, arachidonic acid made up 17.6%, 31.8%, 27.8%, 26.1%, 25.4% and 33.5% of the fatty acid composition of PtdIns from brain, heart, liver, spleen, kidney and ovary, respectively. The most abundant molecular species of PtdIns in all these tissues was 1-stearoyl-2-arachidonoyl. Assay of acyltransferase in liver microsomes of yellowtail showed that arachidonic acid was incorporated into PtdIns more effectively than docosahexaenoic acid and that the latter inhibited incorporation of arachidonic acid into PtdCho without inhibiting the utilization of arachidonic acid for PtdIns. This effect of docosahexaenoic acid was not observed in similar experiments using rat liver microsomes and is thought to contribute to the exclusive utilization of arachidonic acid for acylation to PtdIns in yellowtail. Inositolphospholipids and their hydrolysates are known to act as signaling molecules in cells. The conserved hydrophobic structure of PtdIns (the 1-stearoyl-2-arachidonoyl moiety) may have physiological significance not only in mammals but also in fish."},"publication_date":"2003-04","publication_name":{"en":"European Journal of Biochemistry","ja":"European Journal of Biochemistry"},"volume":"270","number":"7","starting_page":"1466","ending_page":"1473","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1046/j.1432-1033.2003.03512.x"],"issn":["0014-2956"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/12450126","label":"url"},{"@id":"https://www.scopus.com/pages/publications/1842837226","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177235","label":"url"}],"paper_title":{"en":"A lipase-inhibiting protein from lipoxygenase-deficient soybean seeds","ja":"A lipase-inhibiting protein from lipoxygenase-deficient soybean seeds"},"authors":{"en":[{"name":"Satouchi K."},{"name":"Kodama Y."},{"name":"Hirano K."},{"name":"Tanaka Tamotsu"},{"name":"Iwamoto H."}],"ja":[{"name":"Satouchi K."},{"name":"Kodama Y."},{"name":"Hirano K."},{"name":"田中 保"},{"name":"Iwamoto H."}]},"description":{"en":"A lipase-inhibiting protein was isolated from lipoxygenase (LOX)-deficient soybean seeds. The molecular mass of the protein was 56.0-kDa and the N-terminal amino acid was blocked. The protein was identified by peptide mass fingerprinting in combination with matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. The masses of the lysyl endopeptidase-digested peptides of the 56.0-kDa inhibiting protein were almost identical to the calculated masses of the theoretically predicted lysyl endopeptidase-treated peptides of beta-amylase from soybean seed. In a previous paper (Biosci. Biotechnol. Biochem., 62, 1498-1503, 1998), we reported that LOX-1, an isozyme of soybean seed LOX, inhibited hydrolysis of soybean oil by pancreatic lipase. Purified beta-amylase also inhibited lipase activity, although the magnitude of inhibition was weaker than that by LOX-1. Thus, there are at least two lipase-inhibiting proteins, one is a LOX and the other is a beta-amylase, in soybean seed.","ja":"A lipase-inhibiting protein was isolated from lipoxygenase (LOX)-deficient soybean seeds. The molecular mass of the protein was 56.0-kDa and the N-terminal amino acid was blocked. The protein was identified by peptide mass fingerprinting in combination with matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. The masses of the lysyl endopeptidase-digested peptides of the 56.0-kDa inhibiting protein were almost identical to the calculated masses of the theoretically predicted lysyl endopeptidase-treated peptides of beta-amylase from soybean seed. In a previous paper (Biosci. Biotechnol. Biochem., 62, 1498-1503, 1998), we reported that LOX-1, an isozyme of soybean seed LOX, inhibited hydrolysis of soybean oil by pancreatic lipase. Purified beta-amylase also inhibited lipase activity, although the magnitude of inhibition was weaker than that by LOX-1. Thus, there are at least two lipase-inhibiting proteins, one is a LOX and the other is a beta-amylase, in soybean seed."},"publication_date":"2002-10","publication_name":{"en":"Bioscience, Biotechnology, and Biochemistry","ja":"Bioscience, Biotechnology, and Biochemistry"},"volume":"66","number":"10","starting_page":"2154","ending_page":"2160","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1271/bbb.66.2154"],"issn":["0916-8451"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/11982483","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1570854176748304256/","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0036683314","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177236","label":"url"}],"paper_title":{"en":"Human platelets respond differentially to lysophosphatidic acids having a highly unsaturated fatty acyl group and alkyl ether-linked lysophosphatidic acids","ja":"Human platelets respond differentially to lysophosphatidic acids having a highly unsaturated fatty acyl group and alkyl ether-linked lysophosphatidic acids"},"authors":{"en":[{"name":"Tokumura Akira"},{"name":"Shinomiya Junya"},{"name":"Kishimoto Seishi"},{"name":"Tanaka Tamotsu"},{"name":"Kogure Kentaro"},{"name":"Sugiura Takayuki"},{"name":"Satouchi Kiyoshi"},{"name":"Waku Keizo"},{"name":"Fukuzawa Kenji"}],"ja":[{"name":"德村 彰"},{"name":"Shinomiya Junya"},{"name":"Kishimoto Seishi"},{"name":"田中 保"},{"name":"小暮 健太朗"},{"name":"Sugiura Takayuki"},{"name":"Satouchi Kiyoshi"},{"name":"Waku Keizo"},{"name":"福澤 健治"}]},"description":{"en":"Lysophosphatidic acid (LPA) is a physiological agonist that is produced by lysophospholipase D, phospholipase A(1) and phospholipase A(2) in the blood of animals. It exerts diverse biological actions on a broad range of animal cells. Specific receptors for this important agonist have been characterized. In this investigation, for the first time we prepared LPAs having a highly unsaturated fatty acyl group, such as the eicosapentaenoyl or docosahexaenoyl residue, and their acetylated derivatives. Human platelets aggregated more potently in response to the highly unsaturated acyl-LPAs than to LPAs with a C(18) fatty acyl group, such as an oleoyl group, while alkyl ether-linked LPAs (alkyl-LPA) had much stronger aggregating activity. Two positional isomers of LPAs with an arachidonoyl, eicosapentaenoyl or docosahexaenoyl group had equipotent aggregatory activity as well as the positional isomers of their acetylated analogues, indicating that putative LPA receptors could not distinguish the difference between the positional isomers. We found that platelet preparations from two individuals showed no aggregatory response to alkyl-LPAs, although they contained mRNAs for known LPA receptors in the following order of expression level: endothelial differentiation gene (Edg)-4>Edg-7>Edg-2. We also obtained evidence that 2-(p-amylcinnamoyl)amino-4-chlorobenzoic acid (ONO-RS-082), a phospholipase A(2) inhibitor, potentiated alkyl-LPA-induced platelet aggregation, but inhibited highly unsaturated acyl-LPA-induced platelet aggregation. These results indicated that human platelets express acyl-LPA-selective and alkyl-LPA-selective receptors on their plasma membrane.","ja":"Lysophosphatidic acid (LPA) is a physiological agonist that is produced by lysophospholipase D, phospholipase A(1) and phospholipase A(2) in the blood of animals. It exerts diverse biological actions on a broad range of animal cells. Specific receptors for this important agonist have been characterized. In this investigation, for the first time we prepared LPAs having a highly unsaturated fatty acyl group, such as the eicosapentaenoyl or docosahexaenoyl residue, and their acetylated derivatives. Human platelets aggregated more potently in response to the highly unsaturated acyl-LPAs than to LPAs with a C(18) fatty acyl group, such as an oleoyl group, while alkyl ether-linked LPAs (alkyl-LPA) had much stronger aggregating activity. Two positional isomers of LPAs with an arachidonoyl, eicosapentaenoyl or docosahexaenoyl group had equipotent aggregatory activity as well as the positional isomers of their acetylated analogues, indicating that putative LPA receptors could not distinguish the difference between the positional isomers. We found that platelet preparations from two individuals showed no aggregatory response to alkyl-LPAs, although they contained mRNAs for known LPA receptors in the following order of expression level: endothelial differentiation gene (Edg)-4>Edg-7>Edg-2. We also obtained evidence that 2-(p-amylcinnamoyl)amino-4-chlorobenzoic acid (ONO-RS-082), a phospholipase A(2) inhibitor, potentiated alkyl-LPA-induced platelet aggregation, but inhibited highly unsaturated acyl-LPA-induced platelet aggregation. These results indicated that human platelets express acyl-LPA-selective and alkyl-LPA-selective receptors on their plasma membrane."},"publication_date":"2002-08-01","publication_name":{"en":"The Biochemical Journal","ja":"The Biochemical Journal"},"volume":"365","number":"Pt 3","starting_page":"617","ending_page":"628","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1042/BJ20020348"],"issn":["0264-6021"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/11559362","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177234","label":"url"}],"paper_title":{"en":"Metabolic characterization of sciadonic acid (5c,11c,14c-eicosatrienoic acid) as an effective substitute for arachidonate of phosphatidylinositol","ja":"Metabolic characterization of sciadonic acid (5c,11c,14c-eicosatrienoic acid) as an effective substitute for arachidonate of phosphatidylinositol"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Morishige J."},{"name":"Takimoto T."},{"name":"Takai Y."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Morishige J."},{"name":"Takimoto T."},{"name":"Takai Y."},{"name":"Satouchi K."}]},"description":{"en":"Sciadonic acid (20:3 Delta-5,11,14) is an n-6 series trienoic acid that lacks the Delta8 double bond of arachidonic acid. This fatty acid is not converted to arachidonic acid in higher animals. In this study, we characterized the metabolic behavior of sciadonic acid in the process of acylation to phospholipid of HepG2 cells. One of the characteristics of fatty acid compositions of phospholipids in sciadonic acid-supplemented cells is a higher proportion of sciadonic acid in phosphatidylinositol (PtdIns) (27.4%) than in phosphatidylethanolamine (PtdEtn) (23.2%), phosphatidylcholine (PtdCho) (17.3%) and phosphatidylserine (PtdSer) (20.1%). Similarly, the proportion of arachidonic acid was higher in PtdIns (35.8%) than in PtdEtn (29.1%), PtdSer (18.2%) and PtdCho (20.2%) in arachidonic-acid-supplemented cells. The extensive accumulation of sciadonic acid in PtdIns resulted in the enrichment of newly formed 1-stearoyl-2-sciadonoyl molecular species (38%) in PtdIns and caused the reduction in the level of pre-existing arachidonic-acid-containing molecular species. The kinetics of incorporation of sciadonic acid to PtdEtn, PtdSer and PtdIns of cells were similar to those of arachidonic acid. In contrast to sciadonic acid, neither eicosapentaenoic acid (20:5 Delta-5,8,11,14,17) nor juniperonic acid (20:4 Delta-5,11,14,17) accumulated in the PtdIns fraction. Rather, these n-3 series polyunsaturated fatty acids, once incorporated into PtdIns, tended to be excluded from PtdIns. In addition, the level of arachidonic-acid-containing PtdIns molecular species remained unchanged by eicosapentaenoic-acid-supplementation. These results suggest that sciadonic acid or sciadonic-acid-containing glycerides are metabolized in a similar manner to arachidonic acid or arachidonic-acid-containing glyceride in the biosynthesis of PtdIns and that sciadonic acid can effectively modify the molecular species composition of PtdIns in HepG2 cells. In this regard, sciadonic acid will be an interesting experimental tool to clarify the significance of arachidonic acid-residue of PtdIns-origin bioactive lipids.","ja":"Sciadonic acid (20:3 Delta-5,11,14) is an n-6 series trienoic acid that lacks the Delta8 double bond of arachidonic acid. This fatty acid is not converted to arachidonic acid in higher animals. In this study, we characterized the metabolic behavior of sciadonic acid in the process of acylation to phospholipid of HepG2 cells. One of the characteristics of fatty acid compositions of phospholipids in sciadonic acid-supplemented cells is a higher proportion of sciadonic acid in phosphatidylinositol (PtdIns) (27.4%) than in phosphatidylethanolamine (PtdEtn) (23.2%), phosphatidylcholine (PtdCho) (17.3%) and phosphatidylserine (PtdSer) (20.1%). Similarly, the proportion of arachidonic acid was higher in PtdIns (35.8%) than in PtdEtn (29.1%), PtdSer (18.2%) and PtdCho (20.2%) in arachidonic-acid-supplemented cells. The extensive accumulation of sciadonic acid in PtdIns resulted in the enrichment of newly formed 1-stearoyl-2-sciadonoyl molecular species (38%) in PtdIns and caused the reduction in the level of pre-existing arachidonic-acid-containing molecular species. The kinetics of incorporation of sciadonic acid to PtdEtn, PtdSer and PtdIns of cells were similar to those of arachidonic acid. In contrast to sciadonic acid, neither eicosapentaenoic acid (20:5 Delta-5,8,11,14,17) nor juniperonic acid (20:4 Delta-5,11,14,17) accumulated in the PtdIns fraction. Rather, these n-3 series polyunsaturated fatty acids, once incorporated into PtdIns, tended to be excluded from PtdIns. In addition, the level of arachidonic-acid-containing PtdIns molecular species remained unchanged by eicosapentaenoic-acid-supplementation. These results suggest that sciadonic acid or sciadonic-acid-containing glycerides are metabolized in a similar manner to arachidonic acid or arachidonic-acid-containing glyceride in the biosynthesis of PtdIns and that sciadonic acid can effectively modify the molecular species composition of PtdIns in HepG2 cells. In this regard, sciadonic acid will be an interesting experimental tool to clarify the significance of arachidonic acid-residue of PtdIns-origin bioactive lipids."},"publication_date":"2001-09","publication_name":{"en":"European Journal of Biochemistry","ja":"European Journal of Biochemistry"},"volume":"268","number":"18","starting_page":"4928","ending_page":"4939","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1046/j.0014-2956.2001.02423.x"],"issn":["0014-2956"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10864031","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0033945077","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177229","label":"url"}],"paper_title":{"en":"Occurrence of a novel cannabimimetic molecule 2-sciadonoylglycerol (2-eicosa-5',11',14'-trienoylglycerol) in the umbrella pine Sciadopitys veticillata seeds","ja":"Occurrence of a novel cannabimimetic molecule 2-sciadonoylglycerol (2-eicosa-5',11',14'-trienoylglycerol) in the umbrella pine Sciadopitys veticillata seeds"},"authors":{"en":[{"name":"Nakane S."},{"name":"Tanaka Tamotsu"},{"name":"Satouchi K."},{"name":"Kobayashi Y."},{"name":"Sugiura T."}],"ja":[{"name":"Nakane S."},{"name":"田中 保"},{"name":"Satouchi K."},{"name":"Kobayashi Y."},{"name":"Sugiura T."}]},"description":{"en":"The umbrella pine Sciadopitys verticillata seeds were found to contain a substantial amount (16.7 nmol/g) of sciadonic acid (all-cis-5,11,14-eicosatrienoic acid)-containing 2-monoacylglycerol, i.e., 2-sciadonoylglycerol (2-eicosa-5',11',14'-trienoylglycerol). Because the structure of 2-sciadonoylglycerol closely resembles that of 2-arachidonoylglycerol, the endogenous natural ligand for the cannabinoid receptor, we examined whether or not 2-sciadonoylglycerol exhibits cannabimimetic activity using NG108-15 neuroblastomaxglioma hybrid cells which express the cannabinoid CB1 receptor. We found that 2-sciadonoylglycerol induces rapid transient elevation of intracellular free Ca2+ concentration in NG108-15 cells through a cannabinoid CBI receptor-dependent mechanism similar to the case of 2-arachidonoylglycerol, yet the activity of 2-sciadonoylglycerol was apparently lower than that of 2-arachidonoylglycerol. The activity of 2-sciadonoylglycerol was detectable from 3-10 nM, reaching a maximum at around 10 microM. To our knowledge, this is the first report showing the occurrence of a cannabimimetic monoacylglycerol in higher plants.","ja":"The umbrella pine Sciadopitys verticillata seeds were found to contain a substantial amount (16.7 nmol/g) of sciadonic acid (all-cis-5,11,14-eicosatrienoic acid)-containing 2-monoacylglycerol, i.e., 2-sciadonoylglycerol (2-eicosa-5',11',14'-trienoylglycerol). Because the structure of 2-sciadonoylglycerol closely resembles that of 2-arachidonoylglycerol, the endogenous natural ligand for the cannabinoid receptor, we examined whether or not 2-sciadonoylglycerol exhibits cannabimimetic activity using NG108-15 neuroblastomaxglioma hybrid cells which express the cannabinoid CB1 receptor. We found that 2-sciadonoylglycerol induces rapid transient elevation of intracellular free Ca2+ concentration in NG108-15 cells through a cannabinoid CBI receptor-dependent mechanism similar to the case of 2-arachidonoylglycerol, yet the activity of 2-sciadonoylglycerol was apparently lower than that of 2-arachidonoylglycerol. The activity of 2-sciadonoylglycerol was detectable from 3-10 nM, reaching a maximum at around 10 microM. To our knowledge, this is the first report showing the occurrence of a cannabimimetic monoacylglycerol in higher plants."},"publication_date":"2000-06","publication_name":{"en":"Biological & Pharmaceutical Bulletin","ja":"Biological & Pharmaceutical Bulletin"},"volume":"23","number":"6","starting_page":"758","ending_page":"761","languages":["eng"],"referee":true,"identifiers":{"issn":["0918-6158"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10666567","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0033956675","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177225","label":"url"}],"paper_title":{"en":"Purification and regiospecificity of multiple enzyme activities of phospholipase A1 from bonito muscle","ja":"Purification and regiospecificity of multiple enzyme activities of phospholipase A1 from bonito muscle"},"authors":{"en":[{"name":"Hirano K."},{"name":"Okada E."},{"name":"Tanaka Tamotsu"},{"name":"Satouchi K."}],"ja":[{"name":"Hirano K."},{"name":"Okada E."},{"name":"田中 保"},{"name":"Satouchi K."}]},"description":{"en":"Phospholipase A(1) (PLA(1)), which catalyzes the hydrolysis of the sn-1 ester bond of diacyl phospholipids, was purified from 100,000 x g supernatant of bonito muscle to homogeneity by ammonium-sulfate precipitation and four consecutive column chromatographies (DEAE anion-exchange, ether-Toyopeal, hydroxylapatite and Toyopeal HW 50S columns). The final preparation showed a single band above the 67-kDa molecular marker on SDS-PAGE, and the molecular mass was determined to be 71.5 kDa by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using bovine serum albumin as a standard for calibration. The N-terminal 8 amino residues were determined to be Ala-Pro-Ala-Glu-Lys-Val-Lys-Try. Regiospecificity of multiple enzyme activities of the PLA(1) was examined using positionally defined synthetic phosphatidylcholine (PC) and lysophosphatidylcholines (LPC). An acyl ester bond at the sn-1 position of PC was exclusively hydrolyzed by phospholipase activity, and 1-acyl LPC was cleaved to fatty acid and glycerophosphocholine by lysophospholipase (LPL) activity. However, the positional isomer, 2-acyl LPC was a poor substrate for LPL activity. PC/transacylation activity was also observed when excess 2-acyl LPC was supplied in the reaction mixture, and fatty acid at the sn-1 position of donor PC was transferred to the sn-1 position of acceptor LPC. These results demonstrate that the multiple enzyme activities of PLA(1), this is lysophospholipase, transacylase as well as phospholipase, have a strict regiospecificity at the sn-1 position of substrates.","ja":"Phospholipase A(1) (PLA(1)), which catalyzes the hydrolysis of the sn-1 ester bond of diacyl phospholipids, was purified from 100,000 x g supernatant of bonito muscle to homogeneity by ammonium-sulfate precipitation and four consecutive column chromatographies (DEAE anion-exchange, ether-Toyopeal, hydroxylapatite and Toyopeal HW 50S columns). The final preparation showed a single band above the 67-kDa molecular marker on SDS-PAGE, and the molecular mass was determined to be 71.5 kDa by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using bovine serum albumin as a standard for calibration. The N-terminal 8 amino residues were determined to be Ala-Pro-Ala-Glu-Lys-Val-Lys-Try. Regiospecificity of multiple enzyme activities of the PLA(1) was examined using positionally defined synthetic phosphatidylcholine (PC) and lysophosphatidylcholines (LPC). An acyl ester bond at the sn-1 position of PC was exclusively hydrolyzed by phospholipase activity, and 1-acyl LPC was cleaved to fatty acid and glycerophosphocholine by lysophospholipase (LPL) activity. However, the positional isomer, 2-acyl LPC was a poor substrate for LPL activity. PC/transacylation activity was also observed when excess 2-acyl LPC was supplied in the reaction mixture, and fatty acid at the sn-1 position of donor PC was transferred to the sn-1 position of acceptor LPC. These results demonstrate that the multiple enzyme activities of PLA(1), this is lysophospholipase, transacylase as well as phospholipase, have a strict regiospecificity at the sn-1 position of substrates."},"publication_date":"2000-01","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids","ja":"Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"},"volume":"1483","number":"3","starting_page":"325","ending_page":"333","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/S1388-1981(99)00190-0"],"issn":["1388-1981"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10543992","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0033517775","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177223","label":"url"}],"paper_title":{"en":"Non-methylene-interrupted polyunsaturated fatty acids: Effective substitute for arachidonate of phosphatidylinositol","ja":"Non-methylene-interrupted polyunsaturated fatty acids: Effective substitute for arachidonate of phosphatidylinositol"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Izuwa S."},{"name":"Tanaka K."},{"name":"Yamamoto D."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Izuwa S."},{"name":"Tanaka K."},{"name":"Yamamoto D."},{"name":"Satouchi K."}]},"description":{"en":"In mammalian tissues and cells, a characteristic of phosphatidylinositol (PI) is a high abundance of arachidonic acid (AA) relative to the other phospholipids. In this study, we investigated the effects of supplementation of several polyunsaturated fatty acids (PUFAs) on the AA concentration of the PI fraction using a cultured cell system. Neither alpha-linolenic acid nor eicosapentaenoic acid supplement reduced the level of AA in PI of HepG2 cells. In contrast to the n-3 series PUFAs, adding podocarpic acid (20:3, Delta-5,11,14) and pinolenic acid (18:3, Delta-5,9,12) reduced the AA content of the PI fraction from a control value of 15.9% to 7.0 and 8.7%, respectively. In the experiments with pinolenic acid, selective and significant accumulation of 20:3 (Delta-7,11,14), the chain-elongated metabolite of pinolenic acid, was observed in the PI fraction. On the other hand, adding columbinic acid (18:3, Delta-5t,9,12) had no effect on AA content of the PI fraction. Because both podocarpic acid and pinolenic acid are non-methylene-interrupted fatty acids (NMIFAs) that are not converted to AA metabolically, these NMIFAs may be interesting experimental tools for research on the function of PI-origin bioactive lipids.","ja":"In mammalian tissues and cells, a characteristic of phosphatidylinositol (PI) is a high abundance of arachidonic acid (AA) relative to the other phospholipids. In this study, we investigated the effects of supplementation of several polyunsaturated fatty acids (PUFAs) on the AA concentration of the PI fraction using a cultured cell system. Neither alpha-linolenic acid nor eicosapentaenoic acid supplement reduced the level of AA in PI of HepG2 cells. In contrast to the n-3 series PUFAs, adding podocarpic acid (20:3, Delta-5,11,14) and pinolenic acid (18:3, Delta-5,9,12) reduced the AA content of the PI fraction from a control value of 15.9% to 7.0 and 8.7%, respectively. In the experiments with pinolenic acid, selective and significant accumulation of 20:3 (Delta-7,11,14), the chain-elongated metabolite of pinolenic acid, was observed in the PI fraction. On the other hand, adding columbinic acid (18:3, Delta-5t,9,12) had no effect on AA content of the PI fraction. Because both podocarpic acid and pinolenic acid are non-methylene-interrupted fatty acids (NMIFAs) that are not converted to AA metabolically, these NMIFAs may be interesting experimental tools for research on the function of PI-origin bioactive lipids."},"publication_date":"1999-11-02","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"264","number":"3","starting_page":"683","ending_page":"688","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1006/bbrc.1999.1559"],"issn":["0006-291X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/80011179991/","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10429203","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1573387451530325376/","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0033168875","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177230","label":"url"}],"paper_title":{"en":"Biosynthesis of 1,2-dieicosapentaenoyl-sn-glycero-3-phosphocholine in Caenorhabditis elegans","ja":"Biosynthesis of 1,2-dieicosapentaenoyl-sn-glycero-3-phosphocholine in Caenorhabditis elegans"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Izuwa S."},{"name":"Tanaka K."},{"name":"Yamamoto D."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Izuwa S."},{"name":"Tanaka K."},{"name":"Yamamoto D."},{"name":"Satouchi K."}]},"description":{"en":"Previously, we showed that lowering the growth temperature increased the level of eicosapentaenoic acid (EPA) in the phosphatidylcholine (PtdCho) of Caenorhabditis elegans. In this study, we investigated the molecular species composition of PtdCho of C. elegans, with an emphasis on EPA-containing species. C. elegans contained a substantial amount of 1,2-dipolyunsaturated fatty acid-containing PtdCho (1,2-diPUFA-PtdCho) species, such as arachidonic acid/EPA and EPA/EPA, which are unusual phospholipids in higher animals. The EPA/EPA-PtdCho content was significantly increased in C. elegans grown at a low temperature. To examine the possibility that the acyltransferase activity involved in the remodeling of phospholipids accounts for the production of 1,2-diPUFA-PtdCho, we investigated the substrate specificity of this enzyme in C. elegans and found that it did not exhibit a preference for saturated fatty acid for acylation to the sn-1 position of PtdCho. The efficacy of the esterification of EPA to the sn-1 position was almost equal to that of stearic acid. The lack of preference for a saturated fatty acid for acylation to the sn-1 position of PtdCho is thought to result in the existence of the unusual 1,2-diEPA-PtdCho in C. elegans.","ja":"Previously, we showed that lowering the growth temperature increased the level of eicosapentaenoic acid (EPA) in the phosphatidylcholine (PtdCho) of Caenorhabditis elegans. In this study, we investigated the molecular species composition of PtdCho of C. elegans, with an emphasis on EPA-containing species. C. elegans contained a substantial amount of 1,2-dipolyunsaturated fatty acid-containing PtdCho (1,2-diPUFA-PtdCho) species, such as arachidonic acid/EPA and EPA/EPA, which are unusual phospholipids in higher animals. The EPA/EPA-PtdCho content was significantly increased in C. elegans grown at a low temperature. To examine the possibility that the acyltransferase activity involved in the remodeling of phospholipids accounts for the production of 1,2-diPUFA-PtdCho, we investigated the substrate specificity of this enzyme in C. elegans and found that it did not exhibit a preference for saturated fatty acid for acylation to the sn-1 position of PtdCho. The efficacy of the esterification of EPA to the sn-1 position was almost equal to that of stearic acid. The lack of preference for a saturated fatty acid for acylation to the sn-1 position of PtdCho is thought to result in the existence of the unusual 1,2-diEPA-PtdCho in C. elegans."},"publication_date":"1999-07","publication_name":{"en":"European Journal of Biochemistry","ja":"European Journal of Biochemistry"},"volume":"263","number":"1","starting_page":"189","ending_page":"194","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1046/j.1432-1327.1999.00480.x"],"issn":["0014-2956"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/9824288","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0032561416","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177221","label":"url"}],"paper_title":{"en":"Cytosolic lysophosphatidylcholine/transacylase in the production of dipolyunsaturated phosphatidylcholine in bonito muscle","ja":"Cytosolic lysophosphatidylcholine/transacylase in the production of dipolyunsaturated phosphatidylcholine in bonito muscle"},"authors":{"en":[{"name":"Hirano K."},{"name":"Ito H."},{"name":"Morihara H."},{"name":"Tanaka Tamotsu"},{"name":"Satouchi K."}],"ja":[{"name":"Hirano K."},{"name":"Ito H."},{"name":"Morihara H."},{"name":"田中 保"},{"name":"Satouchi K."}]},"description":{"en":"Phosphatidylcholine with docosahexaenoic acid at both sn-1 and sn-2 positions occurs in relatively high abundance in bonito muscle. To explore a possible route for the dipolyunsaturated molecular species, phosphatidylcholine formation from 2-[1-14C]linoleoyl lysophosphatidylcholine was examined using a cytosolic fraction from bonito muscle. The formation of radiolabeled phosphatidylcholine was greatest at 15 degrees C and did not require the presence of cofactors such as CoA and calcium. By DEAE-cellulofine column chromatography, the activity to form phosphatidylcholine was separated from that of phospholipase A1, and the specific activity increased by about 100-fold. The possible involvement of cytosolic lysophosphatidylcholine/transacylase in synthesis of dipolyunsaturated phosphatidylcholine is discussed.","ja":"Phosphatidylcholine with docosahexaenoic acid at both sn-1 and sn-2 positions occurs in relatively high abundance in bonito muscle. To explore a possible route for the dipolyunsaturated molecular species, phosphatidylcholine formation from 2-[1-14C]linoleoyl lysophosphatidylcholine was examined using a cytosolic fraction from bonito muscle. The formation of radiolabeled phosphatidylcholine was greatest at 15 degrees C and did not require the presence of cofactors such as CoA and calcium. By DEAE-cellulofine column chromatography, the activity to form phosphatidylcholine was separated from that of phospholipase A1, and the specific activity increased by about 100-fold. The possible involvement of cytosolic lysophosphatidylcholine/transacylase in synthesis of dipolyunsaturated phosphatidylcholine is discussed."},"publication_date":"1998-10-23","publication_name":{"en":"FEBS Letters","ja":"FEBS Letters"},"volume":"437","number":"3","starting_page":"193","ending_page":"196","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/S0014-5793(98)01226-5"],"issn":["0014-5793"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/9748638","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177216","label":"url"}],"paper_title":{"en":"Methylene-interrupted double bond in polyunsaturated fatty acid is essential structure for metabolism by fatty acid chain elongation system of rat liver","ja":"Methylene-interrupted double bond in polyunsaturated fatty acid is essential structure for metabolism by fatty acid chain elongation system of rat liver"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Hattori T."},{"name":"Kouchi M."},{"name":"Hirano K."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Hattori T."},{"name":"Kouchi M."},{"name":"Hirano K."},{"name":"Satouchi K."}]},"description":{"en":"Some plant oils contain non-methylene-interrupted polyunsaturated fatty acids (NMIFAs). Pinolenic acid (all cis delta-5,9,12/18:3) and columbinic acid (trans,cis,cis delta-5,9,12/18:3) are NMIFAs that exist in pine seed oil and columbine seed oil, respectively. We investigated the double bond position of fatty acid recognized by the fatty acid chain elongation system (FACES) of rat liver using NMIFAs as experimental tools. In the total elongation assay, amounts of C2 unit chain-elongated metabolites of pinolenic acid and columbinic acid were 32% and 11%, respectively, compared to that of gamma-linolenic (all cis delta-6,9,12/18:3) as the substrate. In the condensation reaction assay, the rate limiting step of FACES, the conversion rates of pinolenic acid and columbinic acid to the corresponding C20 beta-keto fatty acids were 19% and 9% of that of gamma-linolenic acid, respectively. The formation of elongated metabolite of podocarpic acid (all cis delta-5,11,14/20:3) was only 7% of that of arachidonic acid (all cis delta-5,8,11,14/20:4). From these results it was concluded that the condensing enzyme of FACES could recognize the methylene-interrupted cis double bond structure vicinal to the carboxyl group in the fatty acid molecule.","ja":"Some plant oils contain non-methylene-interrupted polyunsaturated fatty acids (NMIFAs). Pinolenic acid (all cis delta-5,9,12/18:3) and columbinic acid (trans,cis,cis delta-5,9,12/18:3) are NMIFAs that exist in pine seed oil and columbine seed oil, respectively. We investigated the double bond position of fatty acid recognized by the fatty acid chain elongation system (FACES) of rat liver using NMIFAs as experimental tools. In the total elongation assay, amounts of C2 unit chain-elongated metabolites of pinolenic acid and columbinic acid were 32% and 11%, respectively, compared to that of gamma-linolenic (all cis delta-6,9,12/18:3) as the substrate. In the condensation reaction assay, the rate limiting step of FACES, the conversion rates of pinolenic acid and columbinic acid to the corresponding C20 beta-keto fatty acids were 19% and 9% of that of gamma-linolenic acid, respectively. The formation of elongated metabolite of podocarpic acid (all cis delta-5,11,14/20:3) was only 7% of that of arachidonic acid (all cis delta-5,8,11,14/20:4). From these results it was concluded that the condensing enzyme of FACES could recognize the methylene-interrupted cis double bond structure vicinal to the carboxyl group in the fatty acid molecule."},"publication_date":"1998-08-28","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism","ja":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism"},"volume":"1393","number":"2-3","starting_page":"299","ending_page":"306","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/S0005-2760(98)00084-8"],"issn":["0005-2760"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/9757555","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0032135167","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177212","label":"url"}],"paper_title":{"en":"Lipoxygenase-1 from soybean seed inhibiting the activity of pancreatic lipase","ja":"Lipoxygenase-1 from soybean seed inhibiting the activity of pancreatic lipase"},"authors":{"en":[{"name":"Satouchi K."},{"name":"Hirano K."},{"name":"Fijino O."},{"name":"Ikoma M."},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Satouchi K."},{"name":"Hirano K."},{"name":"Fijino O."},{"name":"Ikoma M."},{"name":"田中 保"}]},"description":{"en":"There are some similar characteristics in protein nature between the lipase inhibitor from soybean seed and soybean lipoxygenase-1 (LOX-1). Thus, the inhibiting protein for pancreatic lipase was prepared from defatted soybean meal by the procedure for the isolation of LOX-1 [Axelrod et al., Methods in Enzymology, 71, 441-451 (1981)]. The LOX-1 from soybean seed dose-dependently inhibited the release of fatty acid from a soybean oil emulsion, and the concentration of LOX-1 to cause half inhibition of the lipase activity was 3.2 x 10(-7) M. The LOX-1 obtained from E. coli transfected with a plasmid carrying the soybean LOX-1 gene also inhibited the lipase activity. However, the lipase-inhibiting activity by the LOX-1 was not affected by the presence of nordihydroguaiaretic acid, an inhibitor for LOX, in the reaction mixture. These results show that the soybean LOX-1 inhibits lipase activity regardless of its lipoxygenase activity.","ja":"There are some similar characteristics in protein nature between the lipase inhibitor from soybean seed and soybean lipoxygenase-1 (LOX-1). Thus, the inhibiting protein for pancreatic lipase was prepared from defatted soybean meal by the procedure for the isolation of LOX-1 [Axelrod et al., Methods in Enzymology, 71, 441-451 (1981)]. The LOX-1 from soybean seed dose-dependently inhibited the release of fatty acid from a soybean oil emulsion, and the concentration of LOX-1 to cause half inhibition of the lipase activity was 3.2 x 10(-7) M. The LOX-1 obtained from E. coli transfected with a plasmid carrying the soybean LOX-1 gene also inhibited the lipase activity. However, the lipase-inhibiting activity by the LOX-1 was not affected by the presence of nordihydroguaiaretic acid, an inhibitor for LOX, in the reaction mixture. These results show that the soybean LOX-1 inhibits lipase activity regardless of its lipoxygenase activity."},"publication_date":"1998-08","publication_name":{"en":"Bioscience, Biotechnology, and Biochemistry","ja":"Bioscience, Biotechnology, and Biochemistry"},"volume":"62","number":"8","starting_page":"1498","ending_page":"1503","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1271/bbb.62.1498"],"issn":["0916-8451"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/9498560","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177210","label":"url"}],"paper_title":{"en":"Properties of phospholipase A1/transacylase in the white muscle of Bonito Euthynnus pelamis (Linnaeus)","ja":"Properties of phospholipase A1/transacylase in the white muscle of Bonito Euthynnus pelamis (Linnaeus)"},"authors":{"en":[{"name":"Hirano K."},{"name":"Tanaka A."},{"name":"Yoshizumi K."},{"name":"Tanaka Tamotsu"},{"name":"Satouchi K."}],"ja":[{"name":"Hirano K."},{"name":"Tanaka A."},{"name":"Yoshizumi K."},{"name":"田中 保"},{"name":"Satouchi K."}]},"description":{"en":"The properties of phospholipase A1 (PLA1) obtained from the white muscle of bonito, Euthynnus pelamis (Linnaeus), were examined. The PLA1 activity had a pH optimum from 6.5 to 7.0 for phosphatidylcholine (PC), and calcium ion was not required. The optimum temperature was from 20 to 30 degrees C. When a fatty alcohol was used as an acceptor, a wax ester was produced by transferring a fatty acid at the sn-1 position of the donor's PC. The maximum production of lysophosphatidylcholine was shifted by 0.5 pH units to the acidic side and the pH optimum of wax ester synthesis was from 6.0 to 6.5. The synthesis was independent of calcium ion and Coenzyme A. The transacylation was also observed when 1-lyso-2-acyl-sn-glycero-3-phosphocholine was used as an acceptor. Fatty acid at the sn-1 position of the donor PC was transferred to the unoccupied hydroxy group of the acceptor at the sn-1 position. When 2,3-dipalmitoyl-sn-glycero-1-phosphocholine was used as the acyl donor, a similar amount of palmitic acid was transferred as in the case of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine. However, 1-acyl-2-lyso-sn -glycero-3-phosphocholine, a positional isomer, was a poor acceptor. These results indicate that the transacylation by the PLA1 from bonito muscle is not stereospecific, but is position-specific both for the acyl donor and acceptor.","ja":"The properties of phospholipase A1 (PLA1) obtained from the white muscle of bonito, Euthynnus pelamis (Linnaeus), were examined. The PLA1 activity had a pH optimum from 6.5 to 7.0 for phosphatidylcholine (PC), and calcium ion was not required. The optimum temperature was from 20 to 30 degrees C. When a fatty alcohol was used as an acceptor, a wax ester was produced by transferring a fatty acid at the sn-1 position of the donor's PC. The maximum production of lysophosphatidylcholine was shifted by 0.5 pH units to the acidic side and the pH optimum of wax ester synthesis was from 6.0 to 6.5. The synthesis was independent of calcium ion and Coenzyme A. The transacylation was also observed when 1-lyso-2-acyl-sn-glycero-3-phosphocholine was used as an acceptor. Fatty acid at the sn-1 position of the donor PC was transferred to the unoccupied hydroxy group of the acceptor at the sn-1 position. When 2,3-dipalmitoyl-sn-glycero-1-phosphocholine was used as the acyl donor, a similar amount of palmitic acid was transferred as in the case of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine. However, 1-acyl-2-lyso-sn -glycero-3-phosphocholine, a positional isomer, was a poor acceptor. These results indicate that the transacylation by the PLA1 from bonito muscle is not stereospecific, but is position-specific both for the acyl donor and acceptor."},"publication_date":"1997-12","publication_name":{"en":"The Journal of Biochemistry","ja":"The Journal of Biochemistry"},"volume":"122","number":"6","starting_page":"1160","ending_page":"1166","languages":["eng"],"referee":true,"identifiers":{"issn":["0021-924X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/8934450","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0029855160","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177195","label":"url"}],"paper_title":{"en":"Effects of growth temperature on the fatty acid composition of the free-living nematode Caenorhabditis elegans","ja":"Effects of growth temperature on the fatty acid composition of the free-living nematode Caenorhabditis elegans"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Ikita K."},{"name":"Ashida T."},{"name":"Motoyama Y."},{"name":"Satouchi K."}],"ja":[{"name":"田中 保"},{"name":"Ikita K."},{"name":"Ashida T."},{"name":"Motoyama Y."},{"name":"Satouchi K."}]},"description":{"en":"The effects of growth temperature on the fatty acid compositions of the phosphatidylcholine (PC), phosphatidylethanolamine (PE), and total lipid (TL) fractions of the free-living nematode Caenorhabditis elegans were investigated. A reduction in growth temperature from 25 to 15 degrees C caused the proportions of eicosapentaenoic acid (20:5n-3) to increase from 23.6 to 32.5% in the PC, from 7.4 to 10.8% in the PE, and from 12.9 to 19.9% in the TL fractions. Conversely, the levels of dihomo-gamma-linolenic acid (20:3n-6) and arachidonic acid (20:4n-6) in these phospholipid fractions and the TL fraction both decreased with decreasing growth temperature. Analysis of the positional distribution of fatty acids in the PC fraction revealed that the change in the composition of C20 polyunsaturated fatty acid was obvious in position sn-2. Lowering the growth temperature induced an increase in the level of the diacyl subclass of PE from 58% at 25 degrees C to 71% at 15 degrees C, with a concomitant decrease in the levels of the alkylacyl and alkenylacyl subclass of PE of C. elegans. These changes observed in the phospholipids of C. elegans might be one mechanism for adaptation to low temperature.","ja":"The effects of growth temperature on the fatty acid compositions of the phosphatidylcholine (PC), phosphatidylethanolamine (PE), and total lipid (TL) fractions of the free-living nematode Caenorhabditis elegans were investigated. A reduction in growth temperature from 25 to 15 degrees C caused the proportions of eicosapentaenoic acid (20:5n-3) to increase from 23.6 to 32.5% in the PC, from 7.4 to 10.8% in the PE, and from 12.9 to 19.9% in the TL fractions. Conversely, the levels of dihomo-gamma-linolenic acid (20:3n-6) and arachidonic acid (20:4n-6) in these phospholipid fractions and the TL fraction both decreased with decreasing growth temperature. Analysis of the positional distribution of fatty acids in the PC fraction revealed that the change in the composition of C20 polyunsaturated fatty acid was obvious in position sn-2. Lowering the growth temperature induced an increase in the level of the diacyl subclass of PE from 58% at 25 degrees C to 71% at 15 degrees C, with a concomitant decrease in the levels of the alkylacyl and alkenylacyl subclass of PE of C. elegans. These changes observed in the phospholipids of C. elegans might be one mechanism for adaptation to low temperature."},"publication_date":"1996-11","publication_name":{"en":"Lipids","ja":"Lipids"},"volume":"31","number":"11","starting_page":"1173","ending_page":"1178","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/BF02524292"],"issn":["0024-4201"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/7549088","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177191","label":"url"}],"paper_title":{"en":"Platelet activating factor (PAF)-like phospholipids formed during peroxidation of phosphatidylcholines from different foodstuffs","ja":"Platelet activating factor (PAF)-like phospholipids formed during peroxidation of phosphatidylcholines from different foodstuffs"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"},{"name":"Tsukatani H."}],"ja":[{"name":"田中 保"},{"name":"德村 彰"},{"name":"Tsukatani H."}]},"description":{"en":"Previously, we reported that induction of peroxidation of synthetic phosphatidylcholines (PCs) containing a polyunsaturated fatty acid by Fe(2+)-EDTA in the presence of ascorbate resulted in the formation of four types of PCs with an sn-2-oxidatively fragmented acyl group, which had platelet-aggregating activity due to interaction with platelet-activating factor (PAF) receptors. These PCs were compounds with a short-chain monocarboxylate, omega-hydroxymonocarboxylate, dicarboxylate, and dicarboxylate semialdehyde residue, respectively. In this study, we investigated the PAF-like lipids formed during peroxidation of PCs from hen egg yolk, salmon roe, sea urchin eggs, and krill in an FeSO4/EDTA/ascorbate system. The platelet-aggregating activities of these oxidized PCs were all inhibited by FR-900452, an antagonist of PAF. The activity of oxidized krill PC, which was equivalent of 89.8 +/- 8.8 pmol 16:0-PAF/mumol of starting PC, was about 5 times those of oxidized PCs from salmon roe and sea urchin eggs, and about 50 times that of oxidized hen egg yolk PC. The PAF-like phospholipids that had different combinations of long-chain alkyl or acyl groups with one of the above four types of short-chain acyl groups were identified by gas chromatography-mass spectrometry. The results indicated that foodstuffs that are rich in 1-O-alkyl-2-docosahexaenoyl-sn-glycero-3-phosphocholine are potential sources of compounds with high PAF-like activity formed by deleterious lipid peroxidation.","ja":"Previously, we reported that induction of peroxidation of synthetic phosphatidylcholines (PCs) containing a polyunsaturated fatty acid by Fe(2+)-EDTA in the presence of ascorbate resulted in the formation of four types of PCs with an sn-2-oxidatively fragmented acyl group, which had platelet-aggregating activity due to interaction with platelet-activating factor (PAF) receptors. These PCs were compounds with a short-chain monocarboxylate, omega-hydroxymonocarboxylate, dicarboxylate, and dicarboxylate semialdehyde residue, respectively. In this study, we investigated the PAF-like lipids formed during peroxidation of PCs from hen egg yolk, salmon roe, sea urchin eggs, and krill in an FeSO4/EDTA/ascorbate system. The platelet-aggregating activities of these oxidized PCs were all inhibited by FR-900452, an antagonist of PAF. The activity of oxidized krill PC, which was equivalent of 89.8 +/- 8.8 pmol 16:0-PAF/mumol of starting PC, was about 5 times those of oxidized PCs from salmon roe and sea urchin eggs, and about 50 times that of oxidized hen egg yolk PC. The PAF-like phospholipids that had different combinations of long-chain alkyl or acyl groups with one of the above four types of short-chain acyl groups were identified by gas chromatography-mass spectrometry. The results indicated that foodstuffs that are rich in 1-O-alkyl-2-docosahexaenoyl-sn-glycero-3-phosphocholine are potential sources of compounds with high PAF-like activity formed by deleterious lipid peroxidation."},"publication_date":"1995-08","publication_name":{"en":"Bioscience, Biotechnology, and Biochemistry","ja":"Bioscience, Biotechnology, and Biochemistry"},"volume":"59","number":"8","starting_page":"1389","ending_page":"1393","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1271/bbb.59.1389"],"issn":["0916-8451"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177193","label":"url"}],"paper_title":{"en":"Platelet-activating factor and its structural analogues in the earthworm Eisenia foetida","ja":"Platelet-activating factor and its structural analogues in the earthworm Eisenia foetida"},"authors":{"en":[{"name":"Sugiura T."},{"name":"Yamashita A."},{"name":"Kudo N."},{"name":"Tanaka Tamotsu"},{"name":"Tokumura Akira"}],"ja":[{"name":"Sugiura T."},{"name":"Yamashita A."},{"name":"Kudo N."},{"name":"田中 保"},{"name":"德村 彰"}]},"publication_date":"1995","publication_name":{"en":"Biochim. Biophys. Acta","ja":"Biochim. Biophys. Acta"},"volume":"1258","starting_page":"19","ending_page":"26","languages":["eng"],"referee":true,"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/7918613","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0028073117","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177188","label":"url"}],"paper_title":{"en":"Lysophosphatidylcholine from white muscle of bonito Euthynnus pelamis (Linnaeus): involvement of phospholipase A1 activity for its production","ja":"Lysophosphatidylcholine from white muscle of bonito Euthynnus pelamis (Linnaeus): involvement of phospholipase A1 activity for its production"},"authors":{"en":[{"name":"Satouchi K."},{"name":"Sakaguchi M."},{"name":"Shirakawa M."},{"name":"Hirano K."},{"name":"Tanaka Tamotsu"}],"ja":[{"name":"Satouchi K."},{"name":"Sakaguchi M."},{"name":"Shirakawa M."},{"name":"Hirano K."},{"name":"田中 保"}]},"description":{"en":"A fairly large amount of lysophosphatidylcholine (LPC) was detected in the fresh muscle of bonito Euthynnus pelamis (Linnaeus). The major fatty acid esterified in LPC were highly unsaturated fatty acids, such as docosahexaenoic and eicosapentaenoic acids, and the form was mainly composed of 1-lyso-2-acyl-sn-glycero-3-phosphocholine (1-LPC). The content of this species continued to increase during 4 months of frozen storage and then decreased. Phospholipase A1 activity detected in the bonito muscle was supposed to be responsible for the accumulation of LPC.","ja":"A fairly large amount of lysophosphatidylcholine (LPC) was detected in the fresh muscle of bonito Euthynnus pelamis (Linnaeus). The major fatty acid esterified in LPC were highly unsaturated fatty acids, such as docosahexaenoic and eicosapentaenoic acids, and the form was mainly composed of 1-lyso-2-acyl-sn-glycero-3-phosphocholine (1-LPC). The content of this species continued to increase during 4 months of frozen storage and then decreased. Phospholipase A1 activity detected in the bonito muscle was supposed to be responsible for the accumulation of LPC."},"publication_date":"1994-10-06","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism","ja":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism"},"volume":"1214","number":"3","starting_page":"303","ending_page":"308","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/0005-2760(94)90077-9"],"issn":["0005-2760"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/8280771","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0027955760","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177189","label":"url"}],"paper_title":{"en":"Platelet-aggregating effects of platelet-activating factor-like phospholipids formed by oxidation of phosphatidylcholines containing an sn-2 polyunsaturated fatty acyl group","ja":"Platelet-aggregating effects of platelet-activating factor-like phospholipids formed by oxidation of phosphatidylcholines containing an sn-2 polyunsaturated fatty acyl group"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Iimori H."},{"name":"Tsukatani H."},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Iimori H."},{"name":"Tsukatani H."},{"name":"德村 彰"}]},"description":{"en":"Previously, we reported the formation of four kinds of phosphatidylcholines (PC) with a short-chain monocarboxylate, dicarboxylate, dicarboxylate semialdehyde or omega-hydroxymonocarboxylate group by oxidation of PCs containing polyunsaturated fatty acid (PUFA) in an FeSO4/ascorbate/EDTA system. In this study, we identified these novel phospholipids by GC-MS as oxidation products of two alkyl ether-linked PCs, 1-O-hexadecyl-2-docosahexaenoyl and 1-O-hexadecyl-2-arachidonoyl-sn-glycero-3- phosphocholine (GPC). The sn-2-acyl moieties of oxidatively fragmented PCs derived from PCs containing docosahexaenoate were one methylene unit shorter than those detected as major oxidation products of PCs containing arachidonate. The platelet-aggregations induced by the oxidized PCs were all inhibited by FR-900452, an antagonist of platelet activating factor (PAF). The PAF-like activity of oxidized 1-O-hexadecyl-2-docosahexaenoyl-GPC, which was equivalent of 1372 +/- 262 pmol 16:0-PAF/mumol starting PC, was 5 times that of oxidized 1-O-hexadecyl-2-arachidonoyl-GPC and 150 times that of oxidized 1-palmitoyl-2-docosahexaenoyl-GPC, suggesting that both an sn-1-alkyl ether linkage and an sn-2-acyl group with a short chain length are important structural requirements for induction of platelet aggregation. These possibilities were confirmed by experiments on the platelet-aggregating activities of synthetic PAF-like compounds. Quantitative measurements by GC-MS of PAF-like phospholipids formed by lipid peroxidation and the activities of synthetic PAF-like phospholipids, suggested that the activities of most oxidized PCs containing PUFA were ascribable to those of PCs with an sn-2-short-chain monocarboxylate group.","ja":"Previously, we reported the formation of four kinds of phosphatidylcholines (PC) with a short-chain monocarboxylate, dicarboxylate, dicarboxylate semialdehyde or omega-hydroxymonocarboxylate group by oxidation of PCs containing polyunsaturated fatty acid (PUFA) in an FeSO4/ascorbate/EDTA system. In this study, we identified these novel phospholipids by GC-MS as oxidation products of two alkyl ether-linked PCs, 1-O-hexadecyl-2-docosahexaenoyl and 1-O-hexadecyl-2-arachidonoyl-sn-glycero-3- phosphocholine (GPC). The sn-2-acyl moieties of oxidatively fragmented PCs derived from PCs containing docosahexaenoate were one methylene unit shorter than those detected as major oxidation products of PCs containing arachidonate. The platelet-aggregations induced by the oxidized PCs were all inhibited by FR-900452, an antagonist of platelet activating factor (PAF). The PAF-like activity of oxidized 1-O-hexadecyl-2-docosahexaenoyl-GPC, which was equivalent of 1372 +/- 262 pmol 16:0-PAF/mumol starting PC, was 5 times that of oxidized 1-O-hexadecyl-2-arachidonoyl-GPC and 150 times that of oxidized 1-palmitoyl-2-docosahexaenoyl-GPC, suggesting that both an sn-1-alkyl ether linkage and an sn-2-acyl group with a short chain length are important structural requirements for induction of platelet aggregation. These possibilities were confirmed by experiments on the platelet-aggregating activities of synthetic PAF-like compounds. Quantitative measurements by GC-MS of PAF-like phospholipids formed by lipid peroxidation and the activities of synthetic PAF-like phospholipids, suggested that the activities of most oxidized PCs containing PUFA were ascribable to those of PCs with an sn-2-short-chain monocarboxylate group."},"publication_date":"1994-01-03","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism","ja":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism"},"volume":"1210","number":"2","starting_page":"202","ending_page":"208","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/0005-2760(94)90122-8"],"issn":["0005-2760"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177187","label":"url"}],"paper_title":{"en":"Formation of platelet-activating factor-like phospholipids by Fe2+/ascorbate/EDTA-induced lipid peroxidation","ja":"Formation of platelet-activating factor-like phospholipids by Fe2+/ascorbate/EDTA-induced lipid peroxidation"},"authors":{"en":[{"name":"Tanaka Tamotsu"},{"name":"Minamino H."},{"name":"Unezaki S."},{"name":"Tsukatani H."},{"name":"Tokumura Akira"}],"ja":[{"name":"田中 保"},{"name":"Minamino H."},{"name":"Unezaki S."},{"name":"Tsukatani H."},{"name":"德村 彰"}]},"publication_date":"1994","publication_name":{"en":"Biochim. Biophys. Acta","ja":"Biochim. Biophys. Acta"},"volume":"1210","starting_page":"202","ending_page":"208","languages":["eng"],"referee":true,"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177186","label":"url"}],"paper_title":{"en":"Quantitative analysis of platelet-activating factor in rat brain","ja":"Quantitative analysis of platelet-activating factor in rat brain"},"authors":{"en":[{"name":"Tokumura Akira"},{"name":"Yotsumoto Takashi"},{"name":"Hoshikawa T."},{"name":"Tanaka Tamotsu"},{"name":"Tsukatani Hiroaki"}],"ja":[{"name":"德村 彰"},{"name":"Yotsumoto Takashi"},{"name":"Hoshikawa T."},{"name":"田中 保"},{"name":"Tsukatani Hiroaki"}]},"publication_date":"1992","publication_name":{"en":"Life Sciences","ja":"Life Sciences"},"volume":"51","starting_page":"303","ending_page":"308","languages":["eng"],"referee":true,"published_paper_type":"scientific_journal"},"priority":"input_data"}
{"insert":{"user_id":"1000172314","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/2043133","label":"url"},{"@id":"https://www.scopus.com/pages/publications/0025783982","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=177181","label":"url"}],"paper_title":{"en":"Identification of sn-2-ω-hydroxycarboxylate-containing phospholipids in a lipid extract from bovine brain","ja":"Identification of sn-2-ω-hydroxycarboxylate-containing phospholipids in a lipid extract from bovine brain"},"authors":{"en":[{"name":"Tokumura Akira"},{"name":"Tanaka Tamotsu"},{"name":"Yotsumoto Takashi"},{"name":"Tsukatani Hiroaki"}],"ja":[{"name":"德村 彰"},{"name":"田中 保"},{"name":"Yotsumoto Takashi"},{"name":"Tsukatani Hiroaki"}]},"description":{"en":"Phospholipids having both a long-chain acyl (palmitoyl or stearoyl) and a short-chain hydroxycarboxylyl (C3-C9) residue were identified by GC-MS in a fraction with PAF-like activity from a bovine brain lipid extract. The hydroxyl group in the hydroxycarboxylate residue was determined to be at the omega-position by comparison of the mass spectra of the tert-butyl-dimethylsilyl derivatives of these compounds with those of synthetic hydroxybutyrate-containing phosphatidylcholines. The co-existence of short-chain hydroxycarboxylate-, monocarboxylate- and dicarboxylate-containing phospholipids in the bovine brain lipid extract suggested that these compounds were formed by peroxidation of membrane phospholipids, especially phosphatidylcholines.","ja":"Phospholipids having both a long-chain acyl (palmitoyl or stearoyl) and a short-chain hydroxycarboxylyl (C3-C9) residue were identified by GC-MS in a fraction with PAF-like activity from a bovine brain lipid extract. The hydroxyl group in the hydroxycarboxylate residue was determined to be at the omega-position by comparison of the mass spectra of the tert-butyl-dimethylsilyl derivatives of these compounds with those of synthetic hydroxybutyrate-containing phosphatidylcholines. The co-existence of short-chain hydroxycarboxylate-, monocarboxylate- and dicarboxylate-containing phospholipids in the bovine brain lipid extract suggested that these compounds were formed by peroxidation of membrane phospholipids, especially phosphatidylcholines."},"publication_date":"1991-05","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"177","number":"1","starting_page":"466","ending_page":"473","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/0006-291X(91)92007-7"],"issn":["0006-291X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}