=== Generating (published_papers) ===
=== Generating (teaching_experience) ===
=== Generating (education) ===
=== Generating (research_experience) ===
=== Generating (misc) ===
=== Generating (research_projects) ===
=== Generating (books_etc) ===
=== Generating (committee_memberships) ===
=== Generating (awards) ===
=== Generating (association_memberships) ===
=== Generating (presentations) ===
==== begin registerFile(/WWW/pub2/data/ERD/person/264516/researchmap/published_papers.jsonl) ====
line:1, {"insert":{"user_id":"6000005112","type":"published_papers","id":"48343221"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/39457033","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=414990","label":"url"}],"paper_title":{"en":"Rectal Epithelial Stem Cell Kinetics in Acute Radiation Proctitis.","ja":"Rectal Epithelial Stem Cell Kinetics in Acute Radiation Proctitis."},"authors":{"en":[{"name":"SHARMILA GHOSH"},{"name":"Morita Akinori"},{"name":"Nishiyama Yuichi"},{"name":"Sakaue Masahiro"},{"name":"Fujiwara Ken"},{"name":"Morita Daiki"},{"name":"Sonoyama Yuichiro"},{"name":"Higashi Yuichi"},{"name":"Sasatani Megumi"}],"ja":[{"name":"GHOSH SHARMILA"},{"name":"森田 明典"},{"name":"西山 祐一"},{"name":"阪上 昌弘"},{"name":"藤原 健"},{"name":"森田 大貴"},{"name":"園山 雄一郎"},{"name":"東 優一"},{"name":"笹谷 めぐみ"}]},"publication_date":"2024-10-19","publication_name":{"en":"International Journal of Molecular Sciences","ja":"International Journal of Molecular Sciences"},"volume":"Vol.25","number":"No.20","starting_page":"11252","ending_page":"11252","languages":["eng"],"referee":true,"invited":true,"identifiers":{"doi":["10.3390/ijms252011252"],"issn":["1422-0067"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:2, {"insert":{"user_id":"6000005112","type":"published_papers","id":"37853500"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/35635928","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=386244","label":"url"}],"paper_title":{"en":"Design, synthesis and biological evaluation of 2-pyrrolone derivatives as radioprotectors.","ja":"Design, synthesis and biological evaluation of 2-pyrrolone derivatives as radioprotectors."},"authors":{"en":[{"name":"Satoh Hidetoshi"},{"name":"Ochi Shintaroh"},{"name":"Mizuno Kosuke"},{"name":"Saga Yutaka"},{"name":"Ujita Shohei"},{"name":"Toyoda Mihiro"},{"name":"Nishiyama Yuichi"},{"name":"Tada Kasumi"},{"name":"Matsushita Yosuke"},{"name":"Deguchi Yuichi"},{"name":"Suzuki Keiji"},{"name":"Tanaka Yoshimasa"},{"name":"Ueda Hiroshi"},{"name":"Inaba Toshiya"},{"name":"Hosoi Yoshio"},{"name":"Morita Akinori"},{"name":"Aoki Shin"}],"ja":[{"name":"Satoh Hidetoshi"},{"name":"越智 進太郎"},{"name":"Mizuno Kosuke"},{"name":"Saga Yutaka"},{"name":"氏田 将平"},{"name":"豊田 美裕"},{"name":"西山 祐一"},{"name":"多田 佳寿美"},{"name":"松下 洋輔"},{"name":"Deguchi Yuichi"},{"name":"Suzuki Keiji"},{"name":"Tanaka Yoshimasa"},{"name":"Ueda Hiroshi"},{"name":"Inaba Toshiya"},{"name":"Hosoi Yoshio"},{"name":"森田 明典"},{"name":"Aoki Shin"}]},"description":{"en":"It is known that p53 is an important transcription factor and plays a central role in ionizing radiation (IR)-induced DNA damage responses such as cell cycle arrest, DNA repair and apoptosis. We previously reported that regulating p53 protein is an effective strategy for modulating cell fate by reducing the acute side effects of radiation therapy. Herein, we report on the discovery of STK160830 as a new radioprotector from a chemical library at The University of Tokyo and the design, synthesis and biological evaluation of its derivatives. The radioprotective activity of STK160830 itself and its derivatives that were synthesized in this work was evaluated using a leukemia cell line, MOLT-4 cells as a model of normal cells that express the p53 protein in a structure-activity relationships (SAR) study. The experimental results suggest that a direct relationship exists between the inhibitory effect of these STK160830 derivatives on the expression level of p53 and their radioprotective activity and that the suppression of p53 by STK160830 derivatives contribute to protecting MOLT-4 cells from apoptosis that is induced by exposure to radiation.","ja":"It is known that p53 is an important transcription factor and plays a central role in ionizing radiation (IR)-induced DNA damage responses such as cell cycle arrest, DNA repair and apoptosis. We previously reported that regulating p53 protein is an effective strategy for modulating cell fate by reducing the acute side effects of radiation therapy. Herein, we report on the discovery of STK160830 as a new radioprotector from a chemical library at The University of Tokyo and the design, synthesis and biological evaluation of its derivatives. The radioprotective activity of STK160830 itself and its derivatives that were synthesized in this work was evaluated using a leukemia cell line, MOLT-4 cells as a model of normal cells that express the p53 protein in a structure-activity relationships (SAR) study. The experimental results suggest that a direct relationship exists between the inhibitory effect of these STK160830 derivatives on the expression level of p53 and their radioprotective activity and that the suppression of p53 by STK160830 derivatives contribute to protecting MOLT-4 cells from apoptosis that is induced by exposure to radiation."},"publication_date":"2022-05-09","publication_name":{"en":"Bioorganic & Medicinal Chemistry","ja":"Bioorganic & Medicinal Chemistry"},"volume":"Vol.67","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bmc.2022.116764"],"issn":["1464-3391"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:3, {"insert":{"user_id":"6000005112","type":"published_papers","id":"35590046"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/116405","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/34685458","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=382829","label":"url"}],"paper_title":{"en":"A Novel RNA Synthesis Inhibitor, STK160830, Has Negligible DNA-Intercalating Activity for Triggering A p53 Response, and Can Inhibit p53-Dependent Apoptosis.","ja":"A Novel RNA Synthesis Inhibitor, STK160830, Has Negligible DNA-Intercalating Activity for Triggering A p53 Response, and Can Inhibit p53-Dependent Apoptosis."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Ochi Shintaro"},{"name":"Satoh Hidetoshi"},{"name":"Ujita Shohei"},{"name":"Matsushita Yosuke"},{"name":"Tada Kasumi"},{"name":"Toyoda Mihiro"},{"name":"Nishiyama Yuichi"},{"name":"Mizuno Kosuke"},{"name":"Deguchi Yuichi"},{"name":"Suzuki Keiji"},{"name":"Tanaka Yoshimasa"},{"name":"Ueda Hiroshi"},{"name":"Inaba Toshiya"},{"name":"Hosoi Yoshio"},{"name":"Aoki Shin"}],"ja":[{"name":"森田 明典"},{"name":"Ochi Shintaro"},{"name":"Satoh Hidetoshi"},{"name":"Ujita Shohei"},{"name":"松下 洋輔"},{"name":"Tada Kasumi"},{"name":"Toyoda Mihiro"},{"name":"西山 祐一"},{"name":"Mizuno Kosuke"},{"name":"Deguchi Yuichi"},{"name":"Suzuki Keiji"},{"name":"Tanaka Yoshimasa"},{"name":"Ueda Hiroshi"},{"name":"Inaba Toshiya"},{"name":"Hosoi Yoshio"},{"name":"Aoki Shin"}]},"description":{"en":"RNA synthesis inhibitors and protein synthesis inhibitors are useful for investigating whether biological events with unknown mechanisms require transcription or translation; however, the dependence of RNA synthesis has been difficult to verify because many RNA synthesis inhibitors cause adverse events that trigger a p53 response. In this study, we screened a library containing 9600 core compounds and obtained STK160830 that shows anti-apoptotic effects in irradiated wild-type-p53-bearing human T-cell leukemia MOLT-4 cells and murine thymocytes. In many of the p53-impaired cells and p53-knockdown cells tested, STK160830 did not show a remarkable anti-apoptotic effect, suggesting that the anti-apoptotic activity is p53-dependent. In the expression analysis of p53, p53-target gene products, and reference proteins by immunoblotting, STK160830 down-regulated the expression of many of the proteins examined, and the downregulation correlated strongly with its inhibitory effect on cell death. mRNA expression analyses by qPCR and nascent RNA capture kit revealed that STK160830 showed a decreased mRNA expression, which was similar to that induced by the RNA synthesis inhibitor actinomycin D but differed to some extent. Furthermore, unlike other RNA synthesis inhibitors such as actinomycin D, p53 accumulation by STK160830 alone was negligible, and a DNA melting-curve analysis showed very weak DNA-intercalating activity, indicating that STK160830 is a useful inhibitor for RNA synthesis without triggering p53-mediated damage responses.","ja":"RNA synthesis inhibitors and protein synthesis inhibitors are useful for investigating whether biological events with unknown mechanisms require transcription or translation; however, the dependence of RNA synthesis has been difficult to verify because many RNA synthesis inhibitors cause adverse events that trigger a p53 response. In this study, we screened a library containing 9600 core compounds and obtained STK160830 that shows anti-apoptotic effects in irradiated wild-type-p53-bearing human T-cell leukemia MOLT-4 cells and murine thymocytes. In many of the p53-impaired cells and p53-knockdown cells tested, STK160830 did not show a remarkable anti-apoptotic effect, suggesting that the anti-apoptotic activity is p53-dependent. In the expression analysis of p53, p53-target gene products, and reference proteins by immunoblotting, STK160830 down-regulated the expression of many of the proteins examined, and the downregulation correlated strongly with its inhibitory effect on cell death. mRNA expression analyses by qPCR and nascent RNA capture kit revealed that STK160830 showed a decreased mRNA expression, which was similar to that induced by the RNA synthesis inhibitor actinomycin D but differed to some extent. Furthermore, unlike other RNA synthesis inhibitors such as actinomycin D, p53 accumulation by STK160830 alone was negligible, and a DNA melting-curve analysis showed very weak DNA-intercalating activity, indicating that STK160830 is a useful inhibitor for RNA synthesis without triggering p53-mediated damage responses."},"publication_date":"2021-10-15","publication_name":{"en":"Life","ja":"Life"},"volume":"Vol.11","number":"No.10","languages":["eng"],"referee":true,"identifiers":{"doi":["10.3390/life11101087"],"issn":["2075-1729"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:4, {"insert":{"user_id":"6000005112","type":"published_papers","id":"35590047"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/116406","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/34680909","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=382828","label":"url"}],"paper_title":{"en":"Isorhamnetin Promotes 53BP1 Recruitment through the Enhancement of ATM Phosphorylation and Protects Mice from Radiation Gastrointestinal Syndrome.","ja":"Isorhamnetin Promotes 53BP1 Recruitment through the Enhancement of ATM Phosphorylation and Protects Mice from Radiation Gastrointestinal Syndrome."},"authors":{"en":[{"name":"Nishiyama Yuichi"},{"name":"Morita Akinori"},{"name":"Tatsuta Shogo"},{"name":"Kanamaru Misaki"},{"name":"Sakaue Masahiro"},{"name":"Ueda Kenta"},{"name":"Shono Manami"},{"name":"Fujita Rie"},{"name":"Wang Bing"},{"name":"Hosoi Yoshio"},{"name":"Aoki Shin"},{"name":"Sugai Takeshi"}],"ja":[{"name":"西山 祐一"},{"name":"森田 明典"},{"name":"Tatsuta Shogo"},{"name":"Kanamaru Misaki"},{"name":"Sakaue Masahiro"},{"name":"Ueda Kenta"},{"name":"Shono Manami"},{"name":"Fujita Rie"},{"name":"Wang Bing"},{"name":"Hosoi Yoshio"},{"name":"Aoki Shin"},{"name":"Sugai Takeshi"}]},"description":{"en":"Flavonoids are a subclass of polyphenols which are attractive, due to possessing various physiological activities, including a radioprotective effect. Tumor suppressor p53 is a primary regulator in the radiation response and is involved in the pathogenesis of radiation injuries. In this study, we revealed that isorhamnetin inhibited radiation cell death, and investigated its action mechanism focusing on DNA damage response. Although isorhamnetin moderated p53 activity, it promoted phosphorylation of ataxia telangiectasia mutated (ATM) and enhanced 53BP1 recruitment in irradiated cells. The radioprotective effect of isorhamnetin was not observed in the presence of ATM inhibitor, indicating that its protective effect was dependent on ATM. Furthermore, isorhamnetin-treated mice survived gastrointestinal death caused by a lethal dose of abdominal irradiation. These findings suggested that isorhamnetin enhances the ATM-dependent DNA repair process, which is presumably associated with the suppressive effect against GI syndrome.","ja":"Flavonoids are a subclass of polyphenols which are attractive, due to possessing various physiological activities, including a radioprotective effect. Tumor suppressor p53 is a primary regulator in the radiation response and is involved in the pathogenesis of radiation injuries. In this study, we revealed that isorhamnetin inhibited radiation cell death, and investigated its action mechanism focusing on DNA damage response. Although isorhamnetin moderated p53 activity, it promoted phosphorylation of ataxia telangiectasia mutated (ATM) and enhanced 53BP1 recruitment in irradiated cells. The radioprotective effect of isorhamnetin was not observed in the presence of ATM inhibitor, indicating that its protective effect was dependent on ATM. Furthermore, isorhamnetin-treated mice survived gastrointestinal death caused by a lethal dose of abdominal irradiation. These findings suggested that isorhamnetin enhances the ATM-dependent DNA repair process, which is presumably associated with the suppressive effect against GI syndrome."},"publication_date":"2021-09-26","publication_name":{"en":"Genes","ja":"Genes"},"volume":"Vol.12","number":"No.10","languages":["eng"],"referee":true,"identifiers":{"doi":["10.3390/genes12101514"],"issn":["2073-4425"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:5, {"insert":{"user_id":"6000005112","type":"published_papers","id":"32962563"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/116409","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/34125648","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=376642","label":"url"}],"paper_title":{"en":"Evaluation of sodium orthovanadate as a radioprotective agent under total-body irradiation and partial-body irradiation conditions in mice.","ja":"Evaluation of sodium orthovanadate as a radioprotective agent under total-body irradiation and partial-body irradiation conditions in mice."},"authors":{"en":[{"name":"Nishiyama Yuichi"},{"name":"Morita Akinori"},{"name":"Wang Bing"},{"name":"Sakai Takuma"},{"name":"Ramadhani Dwi"},{"name":"Tanaka Kaoru"},{"name":"Sasatani Megumi"},{"name":"Ochi Shintaro"},{"name":"Tominaga Masahide"},{"name":"Ikushima Hitoshi"},{"name":"Ueno Junji"},{"name":"Nenoi Mitsuru"},{"name":"Aoki Shin"}],"ja":[{"name":"西山 祐一"},{"name":"森田 明典"},{"name":"Wang Bing"},{"name":"Sakai Takuma"},{"name":"Ramadhani Dwi"},{"name":"Tanaka Kaoru"},{"name":"Sasatani Megumi"},{"name":"Ochi Shintaro"},{"name":"富永 正英"},{"name":"生島 仁史"},{"name":"上野 淳二"},{"name":"Nenoi Mitsuru"},{"name":"Aoki Shin"}]},"publication_date":"2021-06-14","publication_name":{"en":"International Journal of Radiation Biology","ja":"International Journal of Radiation Biology"},"volume":"Vol.97","number":"No.9","starting_page":"1241","ending_page":"1251","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1080/09553002.2021.1941377"],"issn":["1362-3095"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:6, {"insert":{"user_id":"6000005112","type":"published_papers","id":"33068393"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/34015702","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=376733","label":"url"}],"paper_title":{"en":"Epo-C12 inhibits peroxiredoxin 1 peroxidase activity.","ja":"Epo-C12 inhibits peroxiredoxin 1 peroxidase activity."},"authors":{"en":[{"name":"Yoda Tomoka"},{"name":"Furuta Masateru"},{"name":"Tsutsumi Tomohiko"},{"name":"Ikeda Seiki"},{"name":"Yukizawa Shunsuke"},{"name":"Arai Satoshi"},{"name":"Morita Akinori"},{"name":"Yamatoya Kenji"},{"name":"Nakata Kazuya"},{"name":"Tomoshige Shusuke"},{"name":"Ohgane Kenji"},{"name":"Furuyama Yuuki"},{"name":"Sakaguchi Kengo"},{"name":"Sugawara Fumio"},{"name":"Kobayashi Susumu"},{"name":"Ikekita Masahiko"},{"name":"Kuramochi Kouji"}],"ja":[{"name":"Yoda Tomoka"},{"name":"Furuta Masateru"},{"name":"Tsutsumi Tomohiko"},{"name":"Ikeda Seiki"},{"name":"Yukizawa Shunsuke"},{"name":"Arai Satoshi"},{"name":"森田 明典"},{"name":"Yamatoya Kenji"},{"name":"Nakata Kazuya"},{"name":"Tomoshige Shusuke"},{"name":"Ohgane Kenji"},{"name":"Furuyama Yuuki"},{"name":"Sakaguchi Kengo"},{"name":"Sugawara Fumio"},{"name":"Kobayashi Susumu"},{"name":"Ikekita Masahiko"},{"name":"Kuramochi Kouji"}]},"description":{"en":"in Prx 1. The present study revealed that Prx 1 is one of the target proteins through which Epo-C12 exerts an apoptotic effect in BALL-1 cells.","ja":"in Prx 1. The present study revealed that Prx 1 is one of the target proteins through which Epo-C12 exerts an apoptotic effect in BALL-1 cells."},"publication_date":"2021-05-10","publication_name":{"en":"Bioorganic & Medicinal Chemistry","ja":"Bioorganic & Medicinal Chemistry"},"volume":"Vol.41","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bmc.2021.116203"],"issn":["1464-3391"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:7, {"insert":{"user_id":"6000005112","type":"published_papers","id":"31347502"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/115457","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/33344403","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-85098120572&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=373047","label":"url"}],"paper_title":{"en":"Protective Effects of p53 Regulatory Agents Against High-LET Radiation-Induced Injury in Mice.","ja":"Protective Effects of p53 Regulatory Agents Against High-LET Radiation-Induced Injury in Mice."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Katsube Takanori"},{"name":"Murakami Masahiro"},{"name":"Shimokawa Takashi"},{"name":"Nishiyama Yuichi"},{"name":"Ochi Shintaro"},{"name":"Satoh Hidetoshi"},{"name":"Nenoi Mitsuru"},{"name":"Aoki Shin"}],"ja":[{"name":"森田 明典"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Katsube Takanori"},{"name":"Murakami Masahiro"},{"name":"Shimokawa Takashi"},{"name":"西山 祐一"},{"name":"Ochi Shintaro"},{"name":"Satoh Hidetoshi"},{"name":"Nenoi Mitsuru"},{"name":"Aoki Shin"}]},"description":{"en":"< 0.02), but not iron-ion irradiation, suggesting the moderate relief of the intestinal damage. These results demonstrated the effectiveness of p53 regulators on acute radiation syndrome induced by high-LET radiation.","ja":"< 0.02), but not iron-ion irradiation, suggesting the moderate relief of the intestinal damage. These results demonstrated the effectiveness of p53 regulators on acute radiation syndrome induced by high-LET radiation."},"publication_date":"2020-12-03","publication_name":{"en":"Frontiers in Public Health","ja":"Frontiers in Public Health"},"volume":"Vol.8","languages":["eng"],"referee":true,"identifiers":{"doi":["10.3389/fpubh.2020.601124"],"issn":["2296-2565"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:8, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400525"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/115325","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/32666201","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-85087895196&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=366786","label":"url"}],"paper_title":{"en":"Synergistic anti-tumor activity of miriplatin and radiation through PUMA-mediated apoptosis in hepatocellular carcinoma.","ja":"Synergistic anti-tumor activity of miriplatin and radiation through PUMA-mediated apoptosis in hepatocellular carcinoma."},"authors":{"en":[{"name":"Tanaka Hironori"},{"name":"Okamoto Koichi"},{"name":"Sato Yasushi"},{"name":"Tanaka Takahiro"},{"name":"Tomonari Tetsu"},{"name":"Nakamura Fumika"},{"name":"Fujino Yasuteru"},{"name":"Mitsui Yasuhiro"},{"name":"Miyamoto Hiroshi"},{"name":"Muguruma Naoki"},{"name":"Morita Akinori"},{"name":"Ikushima Hitoshi"},{"name":"Takayama Tetsuji"}],"ja":[{"name":"田中 宏典"},{"name":"岡本 耕一"},{"name":"佐藤 康史"},{"name":"田中 貴大"},{"name":"友成 哲"},{"name":"中村 文香"},{"name":"藤野 泰輝"},{"name":"三井 康裕"},{"name":"宮本 弘志"},{"name":"六車 直樹"},{"name":"森田 明典"},{"name":"生島 仁史"},{"name":"高山 哲治"}]},"description":{"en":"The prognosis for patients with unresectable advanced hepatocellular carcinoma (HCC) is poor. Miriplatin is a hydrophobic platinum compound that has a long retention time in lesions after transarterial chemoembolization (TACE). We investigated anti-tumor activity of miriplatin combined with irradiation on HCC cells, and its underlying mechanism of apoptosis. We also analyzed the effectiveness of miriplatin-TACE and radiotherapy for locally advanced HCC. Human HCC cell lines HepG2 and HuH-7 were treated with DPC (active form of miriplatin) and radiation, and synergy was evaluated using a combination index (CI). Apoptosis-related proteins and cell cycles were analyzed by western blotting and flowcytometry. We retrospectively analyzed treatment outcomes in 10 unresectable HCC patients with vascular/bile duct invasion treated with miriplatin-TACE and radiotherapy. DPC or X-ray irradiation decreased cell viability dose-dependently. DPC plus irradiation decreased cell viability synergistically in both cell lines (CI < 1, respectively). Cleaved PARP expression was induced much more strongly by DPC plus irradiation than by each treatment alone. Expression of p53 up-regulated modulator of apoptosis (PUMA) was significantly induced by the combination, and knockdown of PUMA with siRNA significantly decreased apoptosis in both cell lines. DPC plus irradiation caused sub-G1, G2/M, and S phase cell arrest in those cells. The combination of miriplatin-TACE and radiotherapy showed a high response rate for patients with locally advanced HCC despite small number of patients. Miriplatin plus irradiation had synergistic anti-tumor activity on HCC cells through PUMA-mediated apoptosis and cell cycle arrest. This combination may possibly be effective in treating locally advanced HCC.","ja":"The prognosis for patients with unresectable advanced hepatocellular carcinoma (HCC) is poor. Miriplatin is a hydrophobic platinum compound that has a long retention time in lesions after transarterial chemoembolization (TACE). We investigated anti-tumor activity of miriplatin combined with irradiation on HCC cells, and its underlying mechanism of apoptosis. We also analyzed the effectiveness of miriplatin-TACE and radiotherapy for locally advanced HCC. Human HCC cell lines HepG2 and HuH-7 were treated with DPC (active form of miriplatin) and radiation, and synergy was evaluated using a combination index (CI). Apoptosis-related proteins and cell cycles were analyzed by western blotting and flowcytometry. We retrospectively analyzed treatment outcomes in 10 unresectable HCC patients with vascular/bile duct invasion treated with miriplatin-TACE and radiotherapy. DPC or X-ray irradiation decreased cell viability dose-dependently. DPC plus irradiation decreased cell viability synergistically in both cell lines (CI < 1, respectively). Cleaved PARP expression was induced much more strongly by DPC plus irradiation than by each treatment alone. Expression of p53 up-regulated modulator of apoptosis (PUMA) was significantly induced by the combination, and knockdown of PUMA with siRNA significantly decreased apoptosis in both cell lines. DPC plus irradiation caused sub-G1, G2/M, and S phase cell arrest in those cells. The combination of miriplatin-TACE and radiotherapy showed a high response rate for patients with locally advanced HCC despite small number of patients. Miriplatin plus irradiation had synergistic anti-tumor activity on HCC cells through PUMA-mediated apoptosis and cell cycle arrest. This combination may possibly be effective in treating locally advanced HCC."},"publication_date":"2020-07-14","publication_name":{"en":"Journal of Gastroenterology","ja":"Journal of Gastroenterology"},"volume":"Vol.55","number":"No.11","starting_page":"1072","ending_page":"1086","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s00535-020-01705-8"],"issn":["1435-5922"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:9, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/111999","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28939557","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-85041474121&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=333948","label":"url"}],"paper_title":{"en":"A chemical modulator of p53 transactivation that acts as a radioprotective agonist.","ja":"A chemical modulator of p53 transactivation that acts as a radioprotective agonist."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Takahashi Ippei"},{"name":"Sasatani Megumi"},{"name":"Aoki Shin"},{"name":"Wang Bing"},{"name":"Ariyasu Shinya"},{"name":"Tanaka Kaoru"},{"name":"Yamaguchi Tetsuji"},{"name":"Sawa Akiko"},{"name":"Nishi Yurie"},{"name":"Teraoka Tatsuro"},{"name":"Ujita Shohei"},{"name":"Kawate Yosuke"},{"name":"Yanagawa Chihiro"},{"name":"Tanimoto Keiji"},{"name":"Enomoto Atsushi"},{"name":"Nenoi Mitsuru"},{"name":"Kamiya Kenji"},{"name":"Nagata Yasushi"},{"name":"Hosoi Yoshio"},{"name":"Inaba Toshiya"}],"ja":[{"name":"森田 明典"},{"name":"Takahashi Ippei"},{"name":"Sasatani Megumi"},{"name":"Aoki Shin"},{"name":"Wang Bing"},{"name":"Ariyasu Shinya"},{"name":"Tanaka Kaoru"},{"name":"Yamaguchi Tetsuji"},{"name":"Sawa Akiko"},{"name":"Nishi Yurie"},{"name":"Teraoka Tatsuro"},{"name":"氏田 将平"},{"name":"Kawate Yosuke"},{"name":"柳川 千裕"},{"name":"Tanimoto Keiji"},{"name":"Enomoto Atsushi"},{"name":"Nenoi Mitsuru"},{"name":"Kamiya Kenji"},{"name":"Nagata Yasushi"},{"name":"Hosoi Yoshio"},{"name":"Inaba Toshiya"}]},"description":{"en":"Inhibiting p53-dependent apoptosis by inhibitors of p53 is an effective strategy for preventing radiation-induced damage in hematopoietic lineages, while p53 and p21 also play radioprotective roles in the gastrointestinal epithelium. We previously identified some zinc(II) chelators, including 8-quinolinol derivatives that suppress apoptosis in attempts to discover compounds that target the zinc-binding site in p53. We found that 5-chloro-8-quinolinol (5CHQ) has a unique p53-modulating activity that shifts its transactivation from proapoptotic to protective responses including enhancing p21 induction and suppressing PUMA induction. This p53-modulating activity also influenced p53 and p53-target gene expression in unirradiated cells without inducing DNA damage. The specificity of 5CHQ for p53 and p21 was demonstrated by silencing the expression of each protein. These effects seems to be attributable to the sequence-specific alteration of p53 DNA-binding, as evaluated by chromatin immunoprecipitation and electrophoretic mobility shift assays. In addition, 5-chloro-8-methoxyquinoline itself had no antiapoptotic activity, indicating that the hydroxyl group at the 8-position is required for its antiapoptotic activity. We applied this remarkable agonistic activity to protecting the hematopoietic and gastrointestinal system in mouse irradiation models. The dose-reduction factors of 5CHQ in total-body and abdominally irradiated mice were about 1.2 and 1.3, respectively. 5CHQ effectively protected mouse epithelial stem cells from a lethal dose of abdominal irradiation. Furthermore, the specificity of 5CHQ for p53 in reducing the lethality induced by abdominal irradiation was revealed in Trp53-KO mice. These results indicate that the pharmacological upregulation of radioprotective p53-target genes is an effective strategy for addressing the gastrointestinal syndrome.","ja":"Inhibiting p53-dependent apoptosis by inhibitors of p53 is an effective strategy for preventing radiation-induced damage in hematopoietic lineages, while p53 and p21 also play radioprotective roles in the gastrointestinal epithelium. We previously identified some zinc(II) chelators, including 8-quinolinol derivatives that suppress apoptosis in attempts to discover compounds that target the zinc-binding site in p53. We found that 5-chloro-8-quinolinol (5CHQ) has a unique p53-modulating activity that shifts its transactivation from proapoptotic to protective responses including enhancing p21 induction and suppressing PUMA induction. This p53-modulating activity also influenced p53 and p53-target gene expression in unirradiated cells without inducing DNA damage. The specificity of 5CHQ for p53 and p21 was demonstrated by silencing the expression of each protein. These effects seems to be attributable to the sequence-specific alteration of p53 DNA-binding, as evaluated by chromatin immunoprecipitation and electrophoretic mobility shift assays. In addition, 5-chloro-8-methoxyquinoline itself had no antiapoptotic activity, indicating that the hydroxyl group at the 8-position is required for its antiapoptotic activity. We applied this remarkable agonistic activity to protecting the hematopoietic and gastrointestinal system in mouse irradiation models. The dose-reduction factors of 5CHQ in total-body and abdominally irradiated mice were about 1.2 and 1.3, respectively. 5CHQ effectively protected mouse epithelial stem cells from a lethal dose of abdominal irradiation. Furthermore, the specificity of 5CHQ for p53 in reducing the lethality induced by abdominal irradiation was revealed in Trp53-KO mice. These results indicate that the pharmacological upregulation of radioprotective p53-target genes is an effective strategy for addressing the gastrointestinal syndrome."},"publication_date":"2017-09-22","publication_name":{"en":"Molecular Cancer Therapeutics","ja":"Molecular Cancer Therapeutics"},"volume":"Vol.17","number":"No.2","starting_page":"432","ending_page":"442","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1158/1535-7163.MCT-16-0554"],"issn":["1538-8514"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:10, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400526"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28733865","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=328344","label":"url"}],"paper_title":{"en":"Checkpoint kinase 2 is dispensable for regulation of the p53 response but is required for G2/M arrest and cell survival in cells with p53 defects under heat stress.","ja":"Checkpoint kinase 2 is dispensable for regulation of the p53 response but is required for G2/M arrest and cell survival in cells with p53 defects under heat stress."},"authors":{"en":[{"name":"Furusawa Yukihiro"},{"name":"Yamanouchi Yuka"},{"name":"Iizumi Takashi"},{"name":"Zhao Qing-Li"},{"name":"Mitsuhashi Yohei"},{"name":"Morita Akinori"},{"name":"Enomoto Atushi"},{"name":"Tabuchi Yoshiaki"},{"name":"Kondo Takashi"}],"ja":[{"name":"Furusawa Yukihiro"},{"name":"Yamanouchi Yuka"},{"name":"Iizumi Takashi"},{"name":"Zhao Qing-Li"},{"name":"Mitsuhashi Yohei"},{"name":"森田 明典"},{"name":"Enomoto Atushi"},{"name":"Tabuchi Yoshiaki"},{"name":"Kondo Takashi"}]},"description":{"en":"Hyperthermia induced by heat stress (HS) is known to inhibit proliferation and induce cell death in cancer. We previously demonstrated that checkpoint kinase 1 (Chk1) contributes to G2/M arrest and cell survival under HS; however, the role of Chk2, a functional analog of Chk1, in regulation of the cell cycle and cell death under HS is still unknown. Here, we addressed the role of Chk2 using Molt-4 cells with p53-targeted shRNA (Molt-4/shp53) and parental control cells (Molt-4/V). Chk2 inhibition suppressed C-terminal acetylation of p53 and delayed the induction of p53-target genes in Molt-4/V cells under HS; however, Chk2 inhibition failed to inhibit apoptosis induced by HS, indicating that Chk2 was dispensable for p53-dependent apoptosis under HS. In contrast, Chk2 inhibition abrogated G2/M arrest and promoted cell death induced by HS in HeLa cells and Molt-4/shp53 cells. Thus, we demonstrated for the first time that Chk2 was required for cell cycle arrest and cell survival, particularly in cells with p53 defects under HS. These findings indicated that Chk2 may be a selective target for p53-mutated or -deficient cancer treated with hyperthermia.","ja":"Hyperthermia induced by heat stress (HS) is known to inhibit proliferation and induce cell death in cancer. We previously demonstrated that checkpoint kinase 1 (Chk1) contributes to G2/M arrest and cell survival under HS; however, the role of Chk2, a functional analog of Chk1, in regulation of the cell cycle and cell death under HS is still unknown. Here, we addressed the role of Chk2 using Molt-4 cells with p53-targeted shRNA (Molt-4/shp53) and parental control cells (Molt-4/V). Chk2 inhibition suppressed C-terminal acetylation of p53 and delayed the induction of p53-target genes in Molt-4/V cells under HS; however, Chk2 inhibition failed to inhibit apoptosis induced by HS, indicating that Chk2 was dispensable for p53-dependent apoptosis under HS. In contrast, Chk2 inhibition abrogated G2/M arrest and promoted cell death induced by HS in HeLa cells and Molt-4/shp53 cells. Thus, we demonstrated for the first time that Chk2 was required for cell cycle arrest and cell survival, particularly in cells with p53 defects under HS. These findings indicated that Chk2 may be a selective target for p53-mutated or -deficient cancer treated with hyperthermia."},"publication_date":"2017-07-21","publication_name":{"en":"Apoptosis","ja":"Apoptosis"},"languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s10495-017-1402-2"],"issn":["1573-675X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:11, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28283087","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=323177","label":"url"}],"paper_title":{"en":"Bisdemethoxycurcumin enhances X-ray-induced apoptosis possibly through p53/Bcl-2 pathway.","ja":"Bisdemethoxycurcumin enhances X-ray-induced apoptosis possibly through p53/Bcl-2 pathway."},"authors":{"en":[{"name":"Enomoto Atsushi"},{"name":"Yamada Junko"},{"name":"Morita Akinori"},{"name":"Miyagawa Kiyoshi"}],"ja":[{"name":"Enomoto Atsushi"},{"name":"Yamada Junko"},{"name":"森田 明典"},{"name":"Miyagawa Kiyoshi"}]},"description":{"en":"Bisdemethoxycurcumin (BDMC), which is isolated from the rhizomes of Curcuma longa, has anti-inflammatory and anti-carcinogenic activities. Here we found that BDMC enhanced X-ray-induced apoptosis in human T-cell leukemia MOLT-4 cells. Knockdown of p53 significantly attenuated the radiosensitizing effect of BDMC. However, BDMC did not enhance X-ray-mediated activation of the p53 signaling pathway via p53's transactivation or mitochondrial translocation. On the other hand, BDMC promoted the X-ray-induced dephosphorylation at Ser 70 in Bcl-2's flexible loop regulatory domain and Bcl-2 binding to p53. Overexpressing Bcl-2 completely blocked the BDMC's radiosensitization effect. Our results indicate that BDMC stimulates the dephosphorylation and p53-binding activity of Bcl-2 and suggest that BDMC may induce a neutralization of Bcl-2's anti-apoptotic function, thereby enhancing X-ray-induced apoptosis.","ja":"Bisdemethoxycurcumin (BDMC), which is isolated from the rhizomes of Curcuma longa, has anti-inflammatory and anti-carcinogenic activities. Here we found that BDMC enhanced X-ray-induced apoptosis in human T-cell leukemia MOLT-4 cells. Knockdown of p53 significantly attenuated the radiosensitizing effect of BDMC. However, BDMC did not enhance X-ray-mediated activation of the p53 signaling pathway via p53's transactivation or mitochondrial translocation. On the other hand, BDMC promoted the X-ray-induced dephosphorylation at Ser 70 in Bcl-2's flexible loop regulatory domain and Bcl-2 binding to p53. Overexpressing Bcl-2 completely blocked the BDMC's radiosensitization effect. Our results indicate that BDMC stimulates the dephosphorylation and p53-binding activity of Bcl-2 and suggest that BDMC may induce a neutralization of Bcl-2's anti-apoptotic function, thereby enhancing X-ray-induced apoptosis."},"publication_date":"2017-01-11","publication_name":{"en":"Mutation Research/Genetic Toxicology and Environmental Mutagenesis","ja":"Mutation Research/Genetic Toxicology and Environmental Mutagenesis"},"volume":"Vol.815","starting_page":"1","ending_page":"5","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.mrgentox.2016.12.005"],"issn":["1383-5718"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:12, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/28010925","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-85000351083&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=321936","label":"url"}],"paper_title":{"en":"Effects of chronic restraint-induced stress on radiation-induced chromosomal aberrations in mouse splenocytes.","ja":"Effects of chronic restraint-induced stress on radiation-induced chromosomal aberrations in mouse splenocytes."},"authors":{"en":[{"name":"Katsube Takanori"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Ninomiya Yasuharu"},{"name":"Varès Guillaume"},{"name":"Kawagoshi Taiki"},{"name":"Shiomi Naoko"},{"name":"Kubota Yoshihisa"},{"name":"Liu Qiang"},{"name":"Morita Akinori"},{"name":"Nakajima Tetsuo"},{"name":"Nenoi Mitsuru"}],"ja":[{"name":"Katsube Takanori"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Ninomiya Yasuharu"},{"name":"Varès Guillaume"},{"name":"Kawagoshi Taiki"},{"name":"Shiomi Naoko"},{"name":"Kubota Yoshihisa"},{"name":"Liu Qiang"},{"name":"森田 明典"},{"name":"Nakajima Tetsuo"},{"name":"Nenoi Mitsuru"}]},"description":{"en":"Both ionizing radiation (IR) and psychological stress (PS) cause detrimental effects on humans. A recent study showed that chronic restraint-induced PS (CRIPS) diminished the functions of Trp53 and enhanced radiocarcinogenesis in Trp53-heterozygous (Trp53(+/-)) mice. These findings had a marked impact on the academic field as well as the general public, particularly among residents living in areas radioactively contaminated by nuclear accidents. In an attempt to elucidate the modifying effects of CRIPS on radiation-induced health consequences in Trp53 wild-type (Trp53(+/+)) animals, investigations involving multidisciplinary analyses were performed. We herein demonstrated that CRIPS induced changes in the frequency of IR-induced chromosomal aberrations (CAs) in splenocytes. Five-week-old male Trp53(+/+) C57BL/6J mice were restrained for 6h per day for 28 consecutive days, and total body irradiation (TBI) at a dose of 4Gy was performed on the 8th day. Metaphase chromosome spreads prepared from splenocytes at the end of the 28-day restraint regimen were painted with fluorescence in situ hybridization (FISH) probes for chromosomes 1, 2, and 3. The results obtained showed that CRIPS alone did not induce CAs, while TBI caused significant increases in CAs, mostly translocations. Translocations appeared at a lower frequency in mice exposed to TBI plus CRIPS than in those exposed to TBI alone. No significant differences were observed in the frequencies of the other types of CAs (insertions, dicentrics, and fragments) visualized with FISH between these experimental groups (TBI+CRIPS vs. TBI). These results suggest that CRIPS does not appear to synergize with the clastogenicity of IR.","ja":"Both ionizing radiation (IR) and psychological stress (PS) cause detrimental effects on humans. A recent study showed that chronic restraint-induced PS (CRIPS) diminished the functions of Trp53 and enhanced radiocarcinogenesis in Trp53-heterozygous (Trp53(+/-)) mice. These findings had a marked impact on the academic field as well as the general public, particularly among residents living in areas radioactively contaminated by nuclear accidents. In an attempt to elucidate the modifying effects of CRIPS on radiation-induced health consequences in Trp53 wild-type (Trp53(+/+)) animals, investigations involving multidisciplinary analyses were performed. We herein demonstrated that CRIPS induced changes in the frequency of IR-induced chromosomal aberrations (CAs) in splenocytes. Five-week-old male Trp53(+/+) C57BL/6J mice were restrained for 6h per day for 28 consecutive days, and total body irradiation (TBI) at a dose of 4Gy was performed on the 8th day. Metaphase chromosome spreads prepared from splenocytes at the end of the 28-day restraint regimen were painted with fluorescence in situ hybridization (FISH) probes for chromosomes 1, 2, and 3. The results obtained showed that CRIPS alone did not induce CAs, while TBI caused significant increases in CAs, mostly translocations. Translocations appeared at a lower frequency in mice exposed to TBI plus CRIPS than in those exposed to TBI alone. No significant differences were observed in the frequencies of the other types of CAs (insertions, dicentrics, and fragments) visualized with FISH between these experimental groups (TBI+CRIPS vs. TBI). These results suggest that CRIPS does not appear to synergize with the clastogenicity of IR."},"publication_date":"2016-11-22","publication_name":{"en":"Mutation Research/Genetic Toxicology and Environmental Mutagenesis","ja":"Mutation Research/Genetic Toxicology and Environmental Mutagenesis"},"volume":"Vol.813","starting_page":"18","ending_page":"26","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.mrgentox.2016.11.005"],"issn":["1383-5718"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:13, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400527"},"force":{"see_also":[{"@id":"https://repo.lib.tokushima-u.ac.jp/ja/115539","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/26045492","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-84942306654&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=295312","label":"url"}],"paper_title":{"en":"Chronic restraint-induced stress has little modifying effect on radiation hematopoietic toxicity in mice.","ja":"Chronic restraint-induced stress has little modifying effect on radiation hematopoietic toxicity in mice."},"authors":{"en":[{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Katsube Takanori"},{"name":"Ninomiya Yasuharu"},{"name":"Vares Guillaume"},{"name":"Liu Qiang"},{"name":"Morita Akinori"},{"name":"Nakajima Tetsuo"},{"name":"Nenoi Mitsuru"}],"ja":[{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Katsube Takanori"},{"name":"Ninomiya Yasuharu"},{"name":"Vares Guillaume"},{"name":"Liu Qiang"},{"name":"森田 明典"},{"name":"Nakajima Tetsuo"},{"name":"Nenoi Mitsuru"}]},"description":{"en":"Both radiation and stresses cause detrimental effects on humans. Besides possible health effects resulting directly from radiation exposure, the nuclear plant accident is a cause of social psychological stresses. A recent study showed that chronic restraint-induced stresses (CRIS) attenuated Trp53 functions and increased carcinogenesis susceptibility of Trp53-heterozygous mice to total-body X-irradiation (TBXI), having a big impact on the academic world and a sensational effect on the public, especially the residents living in radioactively contaminated areas. It is important to investigate the possible modification effects from CRIS on radiation-induced health consequences in Trp53 wild-type (Trp53wt) animals. Prior to a carcinogenesis study, effects of TBXI on the hematopoietic system under CRIS were investigated in terms of hematological abnormality in the peripheral blood and residual damage in the bone marrow erythrocytes using a mouse restraint model. Five-week-old male Trp53wt C57BL/6J mice were restrained 6 h per day for 28 consecutive days, and TBXI (4 Gy) was given on the 8th day. Results showed that CRIS alone induced a marked decrease in the red blood cell (RBC) and the white blood cell (WBC) count, while TBXI caused significantly lower counts of RBCs, WBCs and blood platelets, and a lower concentration of hemoglobin regardless of CRIS. CRIS alone did not show any significant effect on erythrocyte proliferation and on induction of micronucleated erythrocytes, whereas TBXI markedly inhibited erythrocyte proliferation and induced a significant increase in the incidences of micronucleated erythrocytes, regardless of CRIS. These findings suggest that CRIS does not have a significant impact on radiation-induced detrimental effects on the hematopoietic system in Trp53wt mice.","ja":"Both radiation and stresses cause detrimental effects on humans. Besides possible health effects resulting directly from radiation exposure, the nuclear plant accident is a cause of social psychological stresses. A recent study showed that chronic restraint-induced stresses (CRIS) attenuated Trp53 functions and increased carcinogenesis susceptibility of Trp53-heterozygous mice to total-body X-irradiation (TBXI), having a big impact on the academic world and a sensational effect on the public, especially the residents living in radioactively contaminated areas. It is important to investigate the possible modification effects from CRIS on radiation-induced health consequences in Trp53 wild-type (Trp53wt) animals. Prior to a carcinogenesis study, effects of TBXI on the hematopoietic system under CRIS were investigated in terms of hematological abnormality in the peripheral blood and residual damage in the bone marrow erythrocytes using a mouse restraint model. Five-week-old male Trp53wt C57BL/6J mice were restrained 6 h per day for 28 consecutive days, and TBXI (4 Gy) was given on the 8th day. Results showed that CRIS alone induced a marked decrease in the red blood cell (RBC) and the white blood cell (WBC) count, while TBXI caused significantly lower counts of RBCs, WBCs and blood platelets, and a lower concentration of hemoglobin regardless of CRIS. CRIS alone did not show any significant effect on erythrocyte proliferation and on induction of micronucleated erythrocytes, whereas TBXI markedly inhibited erythrocyte proliferation and induced a significant increase in the incidences of micronucleated erythrocytes, regardless of CRIS. These findings suggest that CRIS does not have a significant impact on radiation-induced detrimental effects on the hematopoietic system in Trp53wt mice."},"publication_date":"2015-06-04","publication_name":{"en":"Journal of Radiation Research","ja":"Journal of Radiation Research"},"volume":"Vol.56","number":"No.5","starting_page":"760","ending_page":"767","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1093/jrr/rrv030"],"issn":["1349-9157"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:14, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400528"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/25026551","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-84906094043&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=279601","label":"url"}],"paper_title":{"en":"AS-2, a novel inhibitor of p53-dependent apoptosis, prevents apoptotic mitochondrial dysfunction in a transcription-independent manner and protects mice from a lethal dose of ionizing radiation.","ja":"AS-2, a novel inhibitor of p53-dependent apoptosis, prevents apoptotic mitochondrial dysfunction in a transcription-independent manner and protects mice from a lethal dose of ionizing radiation."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Ariyasu Shinya"},{"name":"Wang Bing"},{"name":"Asanuma Tetsuo"},{"name":"Onoda Takayoshi"},{"name":"Sawa Akiko"},{"name":"Tanaka Kaoru"},{"name":"Takahashi Ippei"},{"name":"Togami Shotaro"},{"name":"Nenoi Mitsuru"},{"name":"Inaba Toshiya"},{"name":"Aoki Shin"}],"ja":[{"name":"森田 明典"},{"name":"Ariyasu Shinya"},{"name":"Wang Bing"},{"name":"Asanuma Tetsuo"},{"name":"Onoda Takayoshi"},{"name":"Sawa Akiko"},{"name":"Tanaka Kaoru"},{"name":"Takahashi Ippei"},{"name":"Togami Shotaro"},{"name":"Nenoi Mitsuru"},{"name":"Inaba Toshiya"},{"name":"Aoki Shin"}]},"description":{"en":"In a previous study, we reported that some tetradentate zinc(II) chelators inhibit p53 through the denaturation of its zinc-requiring structure but a chelator, Bispicen, a potent inhibitor of in vitro apoptosis, failed to show any efficient radioprotective effect against irradiated mice because the toxicity of the chelator to mice. The unsuitability of using tetradentate chelators as radioprotectors prompted us to undertake a more extensive search for p53-inhibiting agents that are weaker zinc(II) chelators and therefore less toxic. Here, we show that an 8-hydroxyquinoline (8HQ) derivative, AS-2, suppresses p53-dependent apoptosis through a transcription-independent mechanism. A mechanistic study using cells with different p53 characteristics revealed that the suppressive effect of AS-2 on apoptosis is specifically mediated through p53. In addition, AS-2 was less effective in preventing p53-mediated transcription-dependent events than pifithrin- (PFT), an inhibitor of transcription-independent apoptosis by p53. Fluorescence visualization of the extranuclear distribution of AS-2 also supports that it is ineffective on the transcription-dependent pathway. Further investigations revealed that AS-2 suppressed mitochondrial apoptotic events, such as the mitochondrial release of intermembrane proteins and the loss of mitochondrial membrane potential, although AS-2 resulted in an increase in the mitochondrial translocation of p53 as opposed to the decrease of cytosolic p53, and did not affect the apoptotic interaction of p53 with Bcl-2. AS-2 also protected mice that had been exposed to a lethal dose of ionizing radiation. Our findings indicate that some types of bidentate 8HQ chelators could serve as radioprotectors with no substantial toxicity in vivo.","ja":"In a previous study, we reported that some tetradentate zinc(II) chelators inhibit p53 through the denaturation of its zinc-requiring structure but a chelator, Bispicen, a potent inhibitor of in vitro apoptosis, failed to show any efficient radioprotective effect against irradiated mice because the toxicity of the chelator to mice. The unsuitability of using tetradentate chelators as radioprotectors prompted us to undertake a more extensive search for p53-inhibiting agents that are weaker zinc(II) chelators and therefore less toxic. Here, we show that an 8-hydroxyquinoline (8HQ) derivative, AS-2, suppresses p53-dependent apoptosis through a transcription-independent mechanism. A mechanistic study using cells with different p53 characteristics revealed that the suppressive effect of AS-2 on apoptosis is specifically mediated through p53. In addition, AS-2 was less effective in preventing p53-mediated transcription-dependent events than pifithrin- (PFT), an inhibitor of transcription-independent apoptosis by p53. Fluorescence visualization of the extranuclear distribution of AS-2 also supports that it is ineffective on the transcription-dependent pathway. Further investigations revealed that AS-2 suppressed mitochondrial apoptotic events, such as the mitochondrial release of intermembrane proteins and the loss of mitochondrial membrane potential, although AS-2 resulted in an increase in the mitochondrial translocation of p53 as opposed to the decrease of cytosolic p53, and did not affect the apoptotic interaction of p53 with Bcl-2. AS-2 also protected mice that had been exposed to a lethal dose of ionizing radiation. Our findings indicate that some types of bidentate 8HQ chelators could serve as radioprotectors with no substantial toxicity in vivo."},"publication_date":"2014-07-12","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.450","number":"No.4","starting_page":"1498","ending_page":"1504","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbrc.2014.07.037"],"issn":["1090-2104"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:15, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400529"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/25002230","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-84905560125&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=279506","label":"url"}],"paper_title":{"en":"Design and synthesis of 8-hydroxyquinoline-based radioprotective agents.","ja":"Design and synthesis of 8-hydroxyquinoline-based radioprotective agents."},"authors":{"en":[{"name":"Ariyasu Shinya"},{"name":"Sawa Akiko"},{"name":"Morita Akinori"},{"name":"Hanaya Kengo"},{"name":"Hoshi Misato"},{"name":"Takahashi Ippei"},{"name":"Wang Bing"},{"name":"Aoki Shin"}],"ja":[{"name":"Ariyasu Shinya"},{"name":"Sawa Akiko"},{"name":"森田 明典"},{"name":"Hanaya Kengo"},{"name":"Hoshi Misato"},{"name":"Takahashi Ippei"},{"name":"Wang Bing"},{"name":"Aoki Shin"}]},"description":{"en":"In radiation therapy, adverse side effects are often induced due to the excessive cell death that occurs in radiosensitive normal cells. The radiation-induced cell death of normal cells is caused, at least in part, by apoptosis, which undergoes via activation of p53 and increase in the p53 protein, a zinc-containing transcriptional factor, in response to cellular damage. Therefore, radioprotective drugs that can protect normal cells from radiation and thus suppress adverse side effects would be highly desirable. We report herein on the radioprotective activity of 8-hydroxyquinoline (8HQ) derivatives that were initially designed so as to interact with the Zn(2+) in p53. Indeed, the 5,7-bis(methylaminosulfonyl)-8HQ and 8-methoxyquinoline derivatives considerably protected MOLT-4 cells against -ray radiation (10Gy), accompanied by a low cytotoxicity. However, mechanistic studies revealed that the interaction of these drugs with p53 is weak and the mechanism for inhibiting apoptosis appears to be different from that of previously reported radioprotectors such as bispicen, which inhibits apoptosis via the denaturation of p53 as well as by blocking both transcription-dependent and -independent apoptotic pathways.","ja":"In radiation therapy, adverse side effects are often induced due to the excessive cell death that occurs in radiosensitive normal cells. The radiation-induced cell death of normal cells is caused, at least in part, by apoptosis, which undergoes via activation of p53 and increase in the p53 protein, a zinc-containing transcriptional factor, in response to cellular damage. Therefore, radioprotective drugs that can protect normal cells from radiation and thus suppress adverse side effects would be highly desirable. We report herein on the radioprotective activity of 8-hydroxyquinoline (8HQ) derivatives that were initially designed so as to interact with the Zn(2+) in p53. Indeed, the 5,7-bis(methylaminosulfonyl)-8HQ and 8-methoxyquinoline derivatives considerably protected MOLT-4 cells against -ray radiation (10Gy), accompanied by a low cytotoxicity. However, mechanistic studies revealed that the interaction of these drugs with p53 is weak and the mechanism for inhibiting apoptosis appears to be different from that of previously reported radioprotectors such as bispicen, which inhibits apoptosis via the denaturation of p53 as well as by blocking both transcription-dependent and -independent apoptotic pathways."},"publication_date":"2014-06-18","publication_name":{"en":"Bioorganic & Medicinal Chemistry","ja":"Bioorganic & Medicinal Chemistry"},"volume":"Vol.22","number":"No.15","starting_page":"3891","ending_page":"3905","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bmc.2014.06.017"],"issn":["1464-3391"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:16, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400530"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/24406161","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-84893725571&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=274383","label":"url"}],"paper_title":{"en":"Mitochondria are required for ATM activation by extranuclear oxidative stress in cultured human hepatoblastoma cell line Hep G2 cells.","ja":"Mitochondria are required for ATM activation by extranuclear oxidative stress in cultured human hepatoblastoma cell line Hep G2 cells."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Tanimoto Keiji"},{"name":"Murakami Tomoki"},{"name":"Morinaga Takeshi"},{"name":"Hosoi Yoshio"}],"ja":[{"name":"森田 明典"},{"name":"Tanimoto Keiji"},{"name":"Murakami Tomoki"},{"name":"Morinaga Takeshi"},{"name":"Hosoi Yoshio"}]},"description":{"en":"Ataxia-telangiectasia mutated (ATM) is a serine/threonine protein kinase that plays a central role in DNA damage response (DDR). A recent study reported that oxidized ATM can be active in the absence of DDR. However, the issue of where ATM is activated by oxidative stress remains unclear. Regarding the localization of ATM, two possible locations, namely, mitochondria and peroxisomes are possible. We report herein that ATM can be activated when exposed to hydrogen peroxide without inducing nuclear DDR in Hep G2 cells, and the oxidized cells could be subjected to subcellular fractionation. The first detergent-based fractionation experiment revealed that active, phosphorylated ATM was located in the second fraction, which also contained both mitochondria and peroxisomes. An alternative fractionation method involving homogenization and differential centrifugation, which permits the light membrane fraction containing peroxisomes to be produced, but not mitochondria, revealed that the light membrane fraction contained only traces of ATM. In contrast, the heavy membrane fraction, which mainly contained mitochondrial components, was enriched in ATM and active ATM, suggesting that the oxidative activation of ATM occurs in mitochondria and not in peroxisomes. In Rho 0-Hep G2 cells, which lack mitochondrial DNA and functional mitochondria, ATM failed to respond to hydrogen peroxide, indicating that mitochondria are required for the oxidative activation of ATM. These findings strongly suggest that ATM can be activated in response to oxidative stress in mitochondria and that this occurs in a DDR-independent manner.","ja":"Ataxia-telangiectasia mutated (ATM) is a serine/threonine protein kinase that plays a central role in DNA damage response (DDR). A recent study reported that oxidized ATM can be active in the absence of DDR. However, the issue of where ATM is activated by oxidative stress remains unclear. Regarding the localization of ATM, two possible locations, namely, mitochondria and peroxisomes are possible. We report herein that ATM can be activated when exposed to hydrogen peroxide without inducing nuclear DDR in Hep G2 cells, and the oxidized cells could be subjected to subcellular fractionation. The first detergent-based fractionation experiment revealed that active, phosphorylated ATM was located in the second fraction, which also contained both mitochondria and peroxisomes. An alternative fractionation method involving homogenization and differential centrifugation, which permits the light membrane fraction containing peroxisomes to be produced, but not mitochondria, revealed that the light membrane fraction contained only traces of ATM. In contrast, the heavy membrane fraction, which mainly contained mitochondrial components, was enriched in ATM and active ATM, suggesting that the oxidative activation of ATM occurs in mitochondria and not in peroxisomes. In Rho 0-Hep G2 cells, which lack mitochondrial DNA and functional mitochondria, ATM failed to respond to hydrogen peroxide, indicating that mitochondria are required for the oxidative activation of ATM. These findings strongly suggest that ATM can be activated in response to oxidative stress in mitochondria and that this occurs in a DDR-independent manner."},"publication_date":"2014-01-06","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.443","number":"No.4","starting_page":"1286","ending_page":"1290","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbrc.2013.12.139"],"issn":["1090-2104"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:17, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/24280450","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-84891939016&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=273718","label":"url"}],"paper_title":{"en":"Evaluation of Zinc (II) chelators for inhibiting p53-mediated apoptosis.","ja":"Evaluation of Zinc (II) chelators for inhibiting p53-mediated apoptosis."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Ariyasu Shinya"},{"name":"Ohya Soichiro"},{"name":"Takahashi Ippei"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Uchida Takatoshi"},{"name":"Okazaki Haruna"},{"name":"Hanaya Kengo"},{"name":"Enomoto Atsushi"},{"name":"Nenoi Mitsuru"},{"name":"Ikekita Masahiko"},{"name":"Aoki Shin"},{"name":"Hosoi Yoshio"}],"ja":[{"name":"森田 明典"},{"name":"Ariyasu Shinya"},{"name":"Ohya Soichiro"},{"name":"Takahashi Ippei"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Uchida Takatoshi"},{"name":"Okazaki Haruna"},{"name":"Hanaya Kengo"},{"name":"Enomoto Atsushi"},{"name":"Nenoi Mitsuru"},{"name":"Ikekita Masahiko"},{"name":"Aoki Shin"},{"name":"Hosoi Yoshio"}]},"description":{"en":"In a previous study, we reported that sodium orthovanadate (vanadate) is the first known inhibitor that is capable of protecting mice from death from the radiation-induced gastrointestinal syndrome via its ability to block both transcription-dependent and transcription-independent p53 apoptotic pathways. In this paper, we report that vanadate has a unique activity for inducing the denaturation of p53 relative to other known radioprotective p53 inhibitors, pifithrin- (PFT) and pifithrin-µ (PFTµ). This potent radioprotective effect of vanadate prompted us to undertake a more extensive search for p53 inhibitors that can induce p53 denaturation. Based on the fact that p53 denaturation can be induced by the dissociation of a zinc ion, which is used as a structural factor of p53, we screened some zinc (II) chelators for the suppression of the DNA binding activity of p53 in vitro and the inhibition of radiation-induced p53-dependent apoptosis in MOLT-4 cells. The findings indicate that two of five zinc (II) chelators also suppressed apoptosis. Among the inhibitors tested, Bispicen (N,N'-Bis(2-pyridylmethyl)-1,2-ethanediamine) had the highest inhibition activity. A mechanistic study using cells bearing different p53 status or functions (i.e., p53-knockdown MOLT-4 transformant and its revertants, p53 mutant cells, p53-null cells), and p53-independent apoptotic stimuli revealed that the suppressive effect of Bispicen on apoptosis is specifically mediated through p53. Moreover, Bispicen, similar to vanadate, induces the denaturation of p53 as well as the blocking of both transcription-dependent and -independent apoptotic pathways. Our findings indicate that the use of zinc (II) chelators represent a new approach for protecting against radiation-induced p53-dependent apoptosis through the inhibition of p53-dependent apoptotic pathways.","ja":"In a previous study, we reported that sodium orthovanadate (vanadate) is the first known inhibitor that is capable of protecting mice from death from the radiation-induced gastrointestinal syndrome via its ability to block both transcription-dependent and transcription-independent p53 apoptotic pathways. In this paper, we report that vanadate has a unique activity for inducing the denaturation of p53 relative to other known radioprotective p53 inhibitors, pifithrin- (PFT) and pifithrin-µ (PFTµ). This potent radioprotective effect of vanadate prompted us to undertake a more extensive search for p53 inhibitors that can induce p53 denaturation. Based on the fact that p53 denaturation can be induced by the dissociation of a zinc ion, which is used as a structural factor of p53, we screened some zinc (II) chelators for the suppression of the DNA binding activity of p53 in vitro and the inhibition of radiation-induced p53-dependent apoptosis in MOLT-4 cells. The findings indicate that two of five zinc (II) chelators also suppressed apoptosis. Among the inhibitors tested, Bispicen (N,N'-Bis(2-pyridylmethyl)-1,2-ethanediamine) had the highest inhibition activity. A mechanistic study using cells bearing different p53 status or functions (i.e., p53-knockdown MOLT-4 transformant and its revertants, p53 mutant cells, p53-null cells), and p53-independent apoptotic stimuli revealed that the suppressive effect of Bispicen on apoptosis is specifically mediated through p53. Moreover, Bispicen, similar to vanadate, induces the denaturation of p53 as well as the blocking of both transcription-dependent and -independent apoptotic pathways. Our findings indicate that the use of zinc (II) chelators represent a new approach for protecting against radiation-induced p53-dependent apoptosis through the inhibition of p53-dependent apoptotic pathways."},"publication_date":"2013-11-24","publication_name":{"en":"Oncotarget","ja":"Oncotarget"},"volume":"Vol.4","number":"No.12","starting_page":"2439","ending_page":"2450","languages":["eng"],"referee":true,"identifiers":{"doi":["10.18632/oncotarget.1535"],"issn":["1949-2553"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:18, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400531"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/23886587","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=272592","label":"url"}],"paper_title":{"en":"The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin modulates radiosensitivity by downregulating serine/threonine kinase 38 via Sp1 inhibition.","ja":"The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin modulates radiosensitivity by downregulating serine/threonine kinase 38 via Sp1 inhibition."},"authors":{"en":[{"name":"Enomoto Atsushi"},{"name":"Fukasawa Takemichi"},{"name":"Takamatsu Nobuhiko"},{"name":"Ito Michihiko"},{"name":"Morita Akinori"},{"name":"Hosoi Yoshio"},{"name":"Miyagawa Kiyoshi"}],"ja":[{"name":"Enomoto Atsushi"},{"name":"Fukasawa Takemichi"},{"name":"Takamatsu Nobuhiko"},{"name":"Ito Michihiko"},{"name":"森田 明典"},{"name":"Hosoi Yoshio"},{"name":"Miyagawa Kiyoshi"}]},"description":{"en":"The ansamycin-based HSP90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) combats tumors and has been shown to modulate cellular sensitivity to radiation, prompting researchers to use 17-AAG as a radiosensitizer. 17-AAG causes the degradation of several oncogenic and signaling proteins. We previously demonstrated that oxidative stress activates serine/threonine kinase 38 (STK38), a member of the protein kinase A (PKA)/PKG/PKC-like family. In the present study, we investigated how 17-AAG affects STK38 expression, and evaluated STK38's role in the regulation of radiosensitivity. We found that 17-AAG depleted cellular STK38 and reduced STK38's kinase activity. Importantly, 17-AAG downregulated the stk38 gene expression. Deletion analysis and site-directed mutagenesis experiments demonstrated that Sp1 was required for the stk38 promoter activity. Treatment with 17-AAG inhibited Sp1's binding to the stk38 promoter by decreasing the amount of Sp1 and knocking down Sp1 reduced STK38 expression. Moreover, 17-AAG treatment or STK38 knockdown enhanced the radiosensitivity of HeLa cells. Our data provide a novel mechanism, mediated by stk38 downregulation, by which 17-AAG radiosensitizes cells.","ja":"The ansamycin-based HSP90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) combats tumors and has been shown to modulate cellular sensitivity to radiation, prompting researchers to use 17-AAG as a radiosensitizer. 17-AAG causes the degradation of several oncogenic and signaling proteins. We previously demonstrated that oxidative stress activates serine/threonine kinase 38 (STK38), a member of the protein kinase A (PKA)/PKG/PKC-like family. In the present study, we investigated how 17-AAG affects STK38 expression, and evaluated STK38's role in the regulation of radiosensitivity. We found that 17-AAG depleted cellular STK38 and reduced STK38's kinase activity. Importantly, 17-AAG downregulated the stk38 gene expression. Deletion analysis and site-directed mutagenesis experiments demonstrated that Sp1 was required for the stk38 promoter activity. Treatment with 17-AAG inhibited Sp1's binding to the stk38 promoter by decreasing the amount of Sp1 and knocking down Sp1 reduced STK38 expression. Moreover, 17-AAG treatment or STK38 knockdown enhanced the radiosensitivity of HeLa cells. Our data provide a novel mechanism, mediated by stk38 downregulation, by which 17-AAG radiosensitizes cells."},"publication_date":"2013-07-22","publication_name":{"en":"European Journal of Cancer","ja":"European Journal of Cancer"},"volume":"Vol.49","starting_page":"3547","ending_page":"3558","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.ejca.2013.06.034"],"issn":["1879-0852"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:19, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400532"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/23349341","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265045","label":"url"}],"paper_title":{"en":"Sodium orthovanadate (vanadate), a potent mitigator of radiation-induced damage to the hematopoietic system in mice.","ja":"Sodium orthovanadate (vanadate), a potent mitigator of radiation-induced damage to the hematopoietic system in mice."},"authors":{"en":[{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Morita Akinori"},{"name":"Ninomiya Yasuharu"},{"name":"Maruyama Kouichi"},{"name":"Fujita Kazuko"},{"name":"Hosoi Yoshio"},{"name":"Nenoi Mitsuru"}],"ja":[{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"森田 明典"},{"name":"Ninomiya Yasuharu"},{"name":"Maruyama Kouichi"},{"name":"Fujita Kazuko"},{"name":"Hosoi Yoshio"},{"name":"Nenoi Mitsuru"}]},"description":{"en":"Previous in vitro and in vivo studies have shown that sodium orthovanadate (vanadate), an inorganic vanadium compound, could effectively suppress radiation-induced p53-mediated apoptosis via both transcription-dependent and transcription-independent pathways. As a potent radiation protector administered at a dose of 20 mg/kg body weight (20 mg/kg) prior to total body irradiation (TBI) by intra-peritoneal (ip) injection, it completely protected mice from hematopoietic syndrome and partially from gastrointestinal syndrome. In the present study, radiation mitigation effects from vanadate were investigated by ip injection of vanadate after TBI in mice. Results showed that a single administration of vanadate at a dose of 20 mg/kg markedly improved the 30-day survival rate and the peripheral blood hemogram, relieved bone marrow aplasia and decreased occurrence of the bone marrow micronucleated erythrocytes in the surviving animals. The dose reduction factor was 1.2 when a single dose of 20 mg/kg was administered 15 min after TBI in mice using the 30-day survival test as the endpoint. Results also showed that either doubling the vanadate dose (40 mg/kg) in a single administration or continuing the vanadate treatment (after a single administration at 20 mg/kg) from the following day at a dose of 5 mg/kg per day for 4 consecutive days further significantly improved the efficacy for rescuing bone marrow failure in the 30-day survival test. Taken together, these findings indicate that vanadate would be a potent mitigator suppressing the acute lethality (hematopoietic syndrome) and minimizing the detrimental effects (anhematopoiesis and delayed genotoxic effects) induced by TBI in mice.","ja":"Previous in vitro and in vivo studies have shown that sodium orthovanadate (vanadate), an inorganic vanadium compound, could effectively suppress radiation-induced p53-mediated apoptosis via both transcription-dependent and transcription-independent pathways. As a potent radiation protector administered at a dose of 20 mg/kg body weight (20 mg/kg) prior to total body irradiation (TBI) by intra-peritoneal (ip) injection, it completely protected mice from hematopoietic syndrome and partially from gastrointestinal syndrome. In the present study, radiation mitigation effects from vanadate were investigated by ip injection of vanadate after TBI in mice. Results showed that a single administration of vanadate at a dose of 20 mg/kg markedly improved the 30-day survival rate and the peripheral blood hemogram, relieved bone marrow aplasia and decreased occurrence of the bone marrow micronucleated erythrocytes in the surviving animals. The dose reduction factor was 1.2 when a single dose of 20 mg/kg was administered 15 min after TBI in mice using the 30-day survival test as the endpoint. Results also showed that either doubling the vanadate dose (40 mg/kg) in a single administration or continuing the vanadate treatment (after a single administration at 20 mg/kg) from the following day at a dose of 5 mg/kg per day for 4 consecutive days further significantly improved the efficacy for rescuing bone marrow failure in the 30-day survival test. Taken together, these findings indicate that vanadate would be a potent mitigator suppressing the acute lethality (hematopoietic syndrome) and minimizing the detrimental effects (anhematopoiesis and delayed genotoxic effects) induced by TBI in mice."},"publication_date":"2013-01-24","publication_name":{"en":"Journal of Radiation Research","ja":"Journal of Radiation Research"},"volume":"Vol.54","number":"No.4","starting_page":"620","ending_page":"629","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1093/jrr/rrs140"],"issn":["1349-9157"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:20, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400533"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/22366497","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265046","label":"url"}],"paper_title":{"en":"Inhibition of DNA-dependent protein kinase promotes ultrasound-induced cell death including apoptosis in human leukemia cells.","ja":"Inhibition of DNA-dependent protein kinase promotes ultrasound-induced cell death including apoptosis in human leukemia cells."},"authors":{"en":[{"name":"Furusawa Yukihiro"},{"name":"Fujiwara Yoshisada"},{"name":"Hassan Mariame Ali"},{"name":"Tabuchi Yoshiaki"},{"name":"Morita Akinori"},{"name":"Enomoto Atsushi"},{"name":"Kondo Takashi"}],"ja":[{"name":"Furusawa Yukihiro"},{"name":"Fujiwara Yoshisada"},{"name":"Hassan Mariame Ali"},{"name":"Tabuchi Yoshiaki"},{"name":"森田 明典"},{"name":"Enomoto Atsushi"},{"name":"Kondo Takashi"}]},"description":{"en":"Ultrasound (US) has been shown to induce cell death in cancer cells; however, the underlying mechanism remains elusive. Here, we report a set of novel findings on the molecular mechanism. We found that Akt (also known as protein kinase B), a substrate of DNA-dependent protein kinase (DNA-PK), was phosphorylated in U937 cells nullified with p53 or Molt-4 cells artificially abrogated with p53 after US exposure. On the contrary, Akt phosphorylation was transiently down-regulated then recovered in Molt-4 cells harboring wild-type p53 in US-exposed cells, possibly due to a mutual regulation between p53 and Akt. Inhibition of ataxia-telangiectasia mutated (ATM) or DNA-PK revealed that DNA-PK, rather than ATM, was preferentially involved in Akt phosphorylation and cell survival after US-exposure in all cell lines. These results indicate that DNA-PK plays a protective role against US-induced cell death regardless of p53 phenotype. In conclusion, our findings provide the first delineation of the role of DNA-PK in US-induced cell death and suggest that targeting DNA-PK might be a promising strategy to augment cancer eradication by US.","ja":"Ultrasound (US) has been shown to induce cell death in cancer cells; however, the underlying mechanism remains elusive. Here, we report a set of novel findings on the molecular mechanism. We found that Akt (also known as protein kinase B), a substrate of DNA-dependent protein kinase (DNA-PK), was phosphorylated in U937 cells nullified with p53 or Molt-4 cells artificially abrogated with p53 after US exposure. On the contrary, Akt phosphorylation was transiently down-regulated then recovered in Molt-4 cells harboring wild-type p53 in US-exposed cells, possibly due to a mutual regulation between p53 and Akt. Inhibition of ataxia-telangiectasia mutated (ATM) or DNA-PK revealed that DNA-PK, rather than ATM, was preferentially involved in Akt phosphorylation and cell survival after US-exposure in all cell lines. These results indicate that DNA-PK plays a protective role against US-induced cell death regardless of p53 phenotype. In conclusion, our findings provide the first delineation of the role of DNA-PK in US-induced cell death and suggest that targeting DNA-PK might be a promising strategy to augment cancer eradication by US."},"publication_date":"2012-02-24","publication_name":{"en":"Cancer Letters","ja":"Cancer Letters"},"volume":"Vol.322","number":"No.1","starting_page":"107","ending_page":"112","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.canlet.2012.02.020"],"issn":["1872-7980"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:21, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400534"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/22187327","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265047","label":"url"}],"paper_title":{"en":"Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5.","ja":"Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5."},"authors":{"en":[{"name":"Ohgomori Tomohiro"},{"name":"Nanao Tomohisa"},{"name":"Morita Akinori"},{"name":"Ikekita Masahiko"}],"ja":[{"name":"Ohgomori Tomohiro"},{"name":"Nanao Tomohisa"},{"name":"森田 明典"},{"name":"Ikekita Masahiko"}]},"description":{"en":"Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized type I membrane glycoprotein, and promotes dendritic filopodia formation. Although we have determined the N-glycan structures of ICAM-5 in a previous report, their function is unknown. Here, we produced fifteen ICAM-5 gene constructs, in which each potential N-glycosylation site was mutated, to elucidate the function of the N-glycans of ICAM-5, and observed the effects of transfection of them on a neuronal cell line, Neuro-2a (N2a). Only the N54Q mutant, which is the mutant for the most N-terminal glycosylation site, failed to induce filopodia-like protrusions in N2a cells. Immunofluorescence staining and cell surface biotinylation revealed that N54Q ICAM-5 was confined to the ER and also could not be expressed on the cell surface. This is further supported by the biochemical evidence that almost all N-glycans of N54Q ICAM-5 were digested by Endo glycosidase H and peptide:N-glycanase, indicating that almost all of them retain high-mannose-type structures in ER. In additon, it also failed to form disulfide bonds or functional protein complexes. The stable transformants of N54Q ICAM-5 showed retarded cell growth, but it was interesting that there was no apparent ER stress, because the mutant was sequentially degraded via ER associated degradation pathway by comparing the susceptibilities of the responses to various inhibitors of this pathway in wild-type and N54Q ICAM-5 transfectants. Taken together, the Asn(54)-linked glycan is necessary for normal trafficking and function of ICAM-5, but is unassociated with ER-associated degradation of it.","ja":"Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized type I membrane glycoprotein, and promotes dendritic filopodia formation. Although we have determined the N-glycan structures of ICAM-5 in a previous report, their function is unknown. Here, we produced fifteen ICAM-5 gene constructs, in which each potential N-glycosylation site was mutated, to elucidate the function of the N-glycans of ICAM-5, and observed the effects of transfection of them on a neuronal cell line, Neuro-2a (N2a). Only the N54Q mutant, which is the mutant for the most N-terminal glycosylation site, failed to induce filopodia-like protrusions in N2a cells. Immunofluorescence staining and cell surface biotinylation revealed that N54Q ICAM-5 was confined to the ER and also could not be expressed on the cell surface. This is further supported by the biochemical evidence that almost all N-glycans of N54Q ICAM-5 were digested by Endo glycosidase H and peptide:N-glycanase, indicating that almost all of them retain high-mannose-type structures in ER. In additon, it also failed to form disulfide bonds or functional protein complexes. The stable transformants of N54Q ICAM-5 showed retarded cell growth, but it was interesting that there was no apparent ER stress, because the mutant was sequentially degraded via ER associated degradation pathway by comparing the susceptibilities of the responses to various inhibitors of this pathway in wild-type and N54Q ICAM-5 transfectants. Taken together, the Asn(54)-linked glycan is necessary for normal trafficking and function of ICAM-5, but is unassociated with ER-associated degradation of it."},"publication_date":"2011-12-21","publication_name":{"en":"Glycoconjugate Journal","ja":"Glycoconjugate Journal"},"volume":"Vol.29","number":"No.1","starting_page":"47","ending_page":"55","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1007/s10719-011-9363-0"],"issn":["1573-4986"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:22, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400535"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/21752645","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265048","label":"url"}],"paper_title":{"en":"3-(3-Phenoxybenzyl)amino--carboline: a novel antitumor drug targeting -tubulin.","ja":"3-(3-Phenoxybenzyl)amino--carboline: a novel antitumor drug targeting -tubulin."},"authors":{"en":[{"name":"Ikeda Reiko"},{"name":"Kurosawa Masaki"},{"name":"Okabayashi Takazumi"},{"name":"Takei Ayako"},{"name":"Yoshiwara Masamichi"},{"name":"Kumakura Tadashi"},{"name":"Sakai Norio"},{"name":"Funatsu Osamu"},{"name":"Morita Akinori"},{"name":"Ikekita Masahiko"},{"name":"Nakaike Yumi"},{"name":"Konakahara Takeo"}],"ja":[{"name":"Ikeda Reiko"},{"name":"Kurosawa Masaki"},{"name":"Okabayashi Takazumi"},{"name":"Takei Ayako"},{"name":"Yoshiwara Masamichi"},{"name":"Kumakura Tadashi"},{"name":"Sakai Norio"},{"name":"Funatsu Osamu"},{"name":"森田 明典"},{"name":"Ikekita Masahiko"},{"name":"Nakaike Yumi"},{"name":"Konakahara Takeo"}]},"description":{"en":"3-(3-Phenoxybenzyl)amino--carboline 2h showed extremely-high activity; the IC(50) value was 0.074 M. To verify 2h-induced cell death types, we observed the chromatin condensation, the DNA fragmentation and activated caspase-3 using Hoechst 33342, agarose electrophoresis and western blot, and suggesting 2h-induced cell death type was apoptosis. Flow cytometry showed that 2h-treated cell was induced SubG1 cell population after G2/M cell cycle arrest. In addition, using affinity chromatography and peptide mass fingerprinting, we found that interacting protein with this compound was -tubulin protein.","ja":"3-(3-Phenoxybenzyl)amino--carboline 2h showed extremely-high activity; the IC(50) value was 0.074 M. To verify 2h-induced cell death types, we observed the chromatin condensation, the DNA fragmentation and activated caspase-3 using Hoechst 33342, agarose electrophoresis and western blot, and suggesting 2h-induced cell death type was apoptosis. Flow cytometry showed that 2h-treated cell was induced SubG1 cell population after G2/M cell cycle arrest. In addition, using affinity chromatography and peptide mass fingerprinting, we found that interacting protein with this compound was -tubulin protein."},"publication_date":"2011-06-22","publication_name":{"en":"Bioorganic & Medicinal Chemistry Letters","ja":"Bioorganic & Medicinal Chemistry Letters"},"volume":"Vol.21","number":"No.16","starting_page":"4784","ending_page":"4787","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bmcl.2011.06.061"],"issn":["1464-3405"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:23, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400536"},"force":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/10028111380/","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/21467739","label":"url"},{"@id":"https://cir.nii.ac.jp/crid/1390282680193524864/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265050","label":"url"}],"paper_title":{"en":"Cycloheximide suppresses radiation-induced apoptosis in MOLT-4 cells with Arg72 variant of p53 through translational inhibition of p53 accumulation.","ja":"Cycloheximide suppresses radiation-induced apoptosis in MOLT-4 cells with Arg72 variant of p53 through translational inhibition of p53 accumulation."},"authors":{"en":[{"name":"Ito Azusa"},{"name":"Morita Akinori"},{"name":"Ohya Soichiro"},{"name":"Yamamoto Shinichi"},{"name":"Enomoto Atsushi"},{"name":"Ikekita Masahiko"}],"ja":[{"name":"Ito Azusa"},{"name":"森田 明典"},{"name":"Ohya Soichiro"},{"name":"Yamamoto Shinichi"},{"name":"Enomoto Atsushi"},{"name":"Ikekita Masahiko"}]},"description":{"en":"The human T-cell leukemia cell line MOLT-4 is highly radiosensitive, and thus it is often used as a model of p53-dependent radiation-induced apoptosis. Two branches of the p53-mediated apoptotic pathway are reported: \"transcription-dependent\" and \"transcription-independent.\" However, the relative contribution of each in different types of cells is not yet clearly defined. Moreover, recent studies have shown that the codon 72 polymorphic variants of p53 show different sensitivities to apoptosis signals. The Arg72 variant has a more potent apoptosis-inducing activity in mitochondria than the Pro72 variant. Here, we initially investigated the codon 72 polymorphism of p53 in MOLT-4 cells. Analysis of the p53 exon 4 genomic DNA sequence, which includes codon 72, revealed that MOLT-4 cells are homozygous for the allele encoding Arg72. We next investigated the involvement of the transcription-independent function of p53 using an RNA synthesis inhibitor, actinomycin D (ActD), and a protein synthesis inhibitor, cycloheximide (CHX), and found that the apoptosis was suppressed by CHX but not by ActD. We also revealed that the suppressive effect of CHX on apoptosis was specifically mediated by p53, using a p53-knockdown MOLT-4 transfectant. Furthermore, the suppressive effect of CHX on apoptosis was highly correlated with the suppression of p53 protein accumulation, and less correlated with the suppression of p53 target genes expression. These results indicated that p53 transactivation is not necessary to induce apoptosis, and that p53 protein accumulation itself is both necessary and sufficient to do so.","ja":"The human T-cell leukemia cell line MOLT-4 is highly radiosensitive, and thus it is often used as a model of p53-dependent radiation-induced apoptosis. Two branches of the p53-mediated apoptotic pathway are reported: \"transcription-dependent\" and \"transcription-independent.\" However, the relative contribution of each in different types of cells is not yet clearly defined. Moreover, recent studies have shown that the codon 72 polymorphic variants of p53 show different sensitivities to apoptosis signals. The Arg72 variant has a more potent apoptosis-inducing activity in mitochondria than the Pro72 variant. Here, we initially investigated the codon 72 polymorphism of p53 in MOLT-4 cells. Analysis of the p53 exon 4 genomic DNA sequence, which includes codon 72, revealed that MOLT-4 cells are homozygous for the allele encoding Arg72. We next investigated the involvement of the transcription-independent function of p53 using an RNA synthesis inhibitor, actinomycin D (ActD), and a protein synthesis inhibitor, cycloheximide (CHX), and found that the apoptosis was suppressed by CHX but not by ActD. We also revealed that the suppressive effect of CHX on apoptosis was specifically mediated by p53, using a p53-knockdown MOLT-4 transfectant. Furthermore, the suppressive effect of CHX on apoptosis was highly correlated with the suppression of p53 protein accumulation, and less correlated with the suppression of p53 target genes expression. These results indicated that p53 transactivation is not necessary to induce apoptosis, and that p53 protein accumulation itself is both necessary and sufficient to do so."},"publication_date":"2011-03","publication_name":{"en":"Journal of Radiation Research","ja":"Journal of Radiation Research"},"volume":"Vol.52","number":"No.3","starting_page":"342","ending_page":"350","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1269/jrr.10151"],"issn":["1349-9157"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:24, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265108","label":"url"}],"paper_title":{"en":"Ridaifen-G induces caspase-independent atypical cell death.","ja":"Ridaifen-G induces caspase-independent atypical cell death."},"authors":{"en":[{"name":"A Anlifeire"},{"name":"M Hatori"},{"name":"Morita Akinori"},{"name":"I Shiina"},{"name":"K Nakata"},{"name":"Y Tosaki"},{"name":"Y.-W. Wang"},{"name":"M Ikekita"},{"name":"G Li"}],"ja":[{"name":"A Anlifeire"},{"name":"M Hatori"},{"name":"森田 明典"},{"name":"I Shiina"},{"name":"K Nakata"},{"name":"Y Tosaki"},{"name":"Y.-W. Wang"},{"name":"M Ikekita"},{"name":"G Li"}]},"publication_date":"2011-03-03","publication_name":{"en":"Chinese Journal of Cell Biology","ja":"Chinese Journal of Cell Biology"},"volume":"Vol.33","number":"No.6","starting_page":"635","ending_page":"644","languages":["eng"],"referee":true,"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:25, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400537"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/20226172","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265052","label":"url"}],"paper_title":{"en":"Activin A induces neuronal differentiation and survival via ALK4 in a SMAD-independent manner in a subpopulation of human neuroblastomas.","ja":"Activin A induces neuronal differentiation and survival via ALK4 in a SMAD-independent manner in a subpopulation of human neuroblastomas."},"authors":{"en":[{"name":"Suzuki Kotaro"},{"name":"Kobayashi Tomomi"},{"name":"Funatsu Osamu"},{"name":"Morita Akinori"},{"name":"Ikekita Masahiko"}],"ja":[{"name":"Suzuki Kotaro"},{"name":"Kobayashi Tomomi"},{"name":"Funatsu Osamu"},{"name":"森田 明典"},{"name":"Ikekita Masahiko"}]},"description":{"en":"Activin A is a multifunctional homo-dimeric protein that belongs to the transforming growth factor (TGF)-beta superfamily. In neurons, activin has neuroprotective effects both in vitro and in vivo, but it inhibits neuronal differentiation in some cell lines. Here we report that activin A can promote neuronal differentiation in particular cases. We examined activin A-induced neuronal differentiation and survival in a selected subpopulation of a human neuroblastoma cell line, SK-N-SH, grown in low-serum (differentiation-inducing) conditions. Activin A caused dramatic neurite outgrowth, and increased the expression of neuronal markers and the transactivation of dopamine beta-hydroxylase. We demonstrated that the activin A signal is transduced through the activin A type 1 receptor, ALK4, and transactivates several TGF-beta target genes in a SMAD-independent manner. That is, activin A did not induce the phosphorylation of SMAD2/3, the interaction of SMAD2/3 with SMAD4, the binding of SMAD2/3 to the promoter of TGF-beta target genes, or the accumulation of SMAD2/3 in the nucleus. These results suggest that, in particular cases, activin A can induce neuronal differentiation and support neuronal survival in vitro. These findings may reflect previously unknown functions of activin A in neuronal cells in vivo.","ja":"Activin A is a multifunctional homo-dimeric protein that belongs to the transforming growth factor (TGF)-beta superfamily. In neurons, activin has neuroprotective effects both in vitro and in vivo, but it inhibits neuronal differentiation in some cell lines. Here we report that activin A can promote neuronal differentiation in particular cases. We examined activin A-induced neuronal differentiation and survival in a selected subpopulation of a human neuroblastoma cell line, SK-N-SH, grown in low-serum (differentiation-inducing) conditions. Activin A caused dramatic neurite outgrowth, and increased the expression of neuronal markers and the transactivation of dopamine beta-hydroxylase. We demonstrated that the activin A signal is transduced through the activin A type 1 receptor, ALK4, and transactivates several TGF-beta target genes in a SMAD-independent manner. That is, activin A did not induce the phosphorylation of SMAD2/3, the interaction of SMAD2/3 with SMAD4, the binding of SMAD2/3 to the promoter of TGF-beta target genes, or the accumulation of SMAD2/3 in the nucleus. These results suggest that, in particular cases, activin A can induce neuronal differentiation and support neuronal survival in vitro. These findings may reflect previously unknown functions of activin A in neuronal cells in vivo."},"publication_date":"2010-03-10","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.394","number":"No.3","starting_page":"639","ending_page":"645","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbrc.2010.03.039"],"issn":["1090-2104"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:26, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/20039701","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265054","label":"url"}],"paper_title":{"en":"Design and synthesis of a fluorescent probe for Zn2+, 5,7-bis(N,N-dimethylaminosulfonyl)-8-hydroxyquinoline-pendant 1,4,7,10-tetraazacyclododecane and Zn2+-dependent hydrolytic and Zn2+-independent photochemical reactivation of its benzenesulfonyl-caged derivative.","ja":"Design and synthesis of a fluorescent probe for Zn2+, 5,7-bis(N,N-dimethylaminosulfonyl)-8-hydroxyquinoline-pendant 1,4,7,10-tetraazacyclododecane and Zn2+-dependent hydrolytic and Zn2+-independent photochemical reactivation of its benzenesulfonyl-caged derivative."},"authors":{"en":[{"name":"Ohshima Ryosuke"},{"name":"Kitamura Masanori"},{"name":"Morita Akinori"},{"name":"Shiro Motoo"},{"name":"Yamada Yasuyuki"},{"name":"Ikekita Masahiko"},{"name":"Kimura Eiichi"},{"name":"Aoki Shin"}],"ja":[{"name":"Ohshima Ryosuke"},{"name":"Kitamura Masanori"},{"name":"森田 明典"},{"name":"Shiro Motoo"},{"name":"Yamada Yasuyuki"},{"name":"Ikekita Masahiko"},{"name":"Kimura Eiichi"},{"name":"Aoki Shin"}]},"description":{"en":"We previously reported on a 8-quinolinol-pendant cyclen (L(5)) as a Zn(2+) fluorophore (cyclen = 1,4,7,10-tetraazacyclododecane) and its caged derivative, 8-(benzenesulfonyloxy)-5-(N,N-dimethylaminosulfonyl)quinolin-2-ylmethyl-pendant cyclen (BS-caged-L(5)), which can be reactivated by hydrolysis of benzenesulfonyl group upon complexation with Zn(2+) at neutral pH to give a 1:1 Zn(2+)-L(5) complex (Zn(H(-1)L(5))). We report herein on the synthesis of 5,7-bis(N,N-dimethylaminosulfonyl)-8-hydroxyquinolin-2-ylmethyl-pendant cyclen (L(6)) and its caged derivative (BS-caged-L(6)) for more sensitive and more efficient cell-membrane permeability than those of L(5) and BS-caged-L(5). By potentiometric pH, (1)H NMR, and UV-vis spectroscopic titrations, the deprotonation constants pK(a1)-pK(a6) of H(5)L(6) were determined to be <2, <2, <2, 2.5 +/- 0.1 (for the 8-OH group of the quinoline moiety), 9.7 +/- 0.1, and 10.8 +/- 0.1 at 25 degrees C with I = 0.1 (NaNO(3)). The results of (1)H NMR, potentiometric pH, UV-vis, and fluorescent titrations showed that L(6) rapidly forms a 1:1 complex with Zn(2+) (Zn(H(-1)L(6))), the dissociation constant of which is 50 fM at pH 7.4. The fluorescent emission of Zn(H(-1)L(6)) at 478 nm is 32 times as large as that of L(6) (excitation at 370 nm), and the fluorescent quantum yield of Zn(H(-1)L(6)) (Phi(F) = 0.41) is much greater than that of Zn(H(-1)L(5)) (Phi(F) = 0.044). The BS-caged-L(6) was reactivated by hydrolysis of the benzenesulfonyl moiety more rapidly (completes in 30 min at pH 7.4 at 37 degrees C) than BS-caged-L(5), presumably enabling the practical detection of Zn(2+) in sample solutions and living cells. The photochemical deprotection of BS-caged-L(6) and the cell membrane permeability of L(6) and BS-caged-L(6) are also described.","ja":"We previously reported on a 8-quinolinol-pendant cyclen (L(5)) as a Zn(2+) fluorophore (cyclen = 1,4,7,10-tetraazacyclododecane) and its caged derivative, 8-(benzenesulfonyloxy)-5-(N,N-dimethylaminosulfonyl)quinolin-2-ylmethyl-pendant cyclen (BS-caged-L(5)), which can be reactivated by hydrolysis of benzenesulfonyl group upon complexation with Zn(2+) at neutral pH to give a 1:1 Zn(2+)-L(5) complex (Zn(H(-1)L(5))). We report herein on the synthesis of 5,7-bis(N,N-dimethylaminosulfonyl)-8-hydroxyquinolin-2-ylmethyl-pendant cyclen (L(6)) and its caged derivative (BS-caged-L(6)) for more sensitive and more efficient cell-membrane permeability than those of L(5) and BS-caged-L(5). By potentiometric pH, (1)H NMR, and UV-vis spectroscopic titrations, the deprotonation constants pK(a1)-pK(a6) of H(5)L(6) were determined to be <2, <2, <2, 2.5 +/- 0.1 (for the 8-OH group of the quinoline moiety), 9.7 +/- 0.1, and 10.8 +/- 0.1 at 25 degrees C with I = 0.1 (NaNO(3)). The results of (1)H NMR, potentiometric pH, UV-vis, and fluorescent titrations showed that L(6) rapidly forms a 1:1 complex with Zn(2+) (Zn(H(-1)L(6))), the dissociation constant of which is 50 fM at pH 7.4. The fluorescent emission of Zn(H(-1)L(6)) at 478 nm is 32 times as large as that of L(6) (excitation at 370 nm), and the fluorescent quantum yield of Zn(H(-1)L(6)) (Phi(F) = 0.41) is much greater than that of Zn(H(-1)L(5)) (Phi(F) = 0.044). The BS-caged-L(6) was reactivated by hydrolysis of the benzenesulfonyl moiety more rapidly (completes in 30 min at pH 7.4 at 37 degrees C) than BS-caged-L(5), presumably enabling the practical detection of Zn(2+) in sample solutions and living cells. The photochemical deprotection of BS-caged-L(6) and the cell membrane permeability of L(6) and BS-caged-L(6) are also described."},"publication_date":"2010-02-01","publication_name":{"en":"Inorganic Chemistry","ja":"Inorganic Chemistry"},"volume":"Vol.49","number":"No.3","starting_page":"888","ending_page":"899","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1021/ic901279t"],"issn":["1520-510X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:27, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/20092938","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265105","label":"url"}],"paper_title":{"en":"Edaravone, a known free radical scavenger, enhances X-ray-induced apoptosis at low concentrations.","ja":"Edaravone, a known free radical scavenger, enhances X-ray-induced apoptosis at low concentrations."},"authors":{"en":[{"name":"Sasano N"},{"name":"Enomoto A"},{"name":"Hosoi Y"},{"name":"Katsumura Y"},{"name":"Matsumoto Y"},{"name":"Morita Akinori"},{"name":"Shiraishi K"},{"name":"Miyagawa K"},{"name":"Igaki H"},{"name":"Nakagawa K"}],"ja":[{"name":"Sasano N"},{"name":"Enomoto A"},{"name":"Hosoi Y"},{"name":"Katsumura Y"},{"name":"Matsumoto Y"},{"name":"森田 明典"},{"name":"Shiraishi K"},{"name":"Miyagawa K"},{"name":"Igaki H"},{"name":"Nakagawa K"}]},"description":{"en":"Edaravone has been reported to have a radioprotective effect at high concentrations. We now report that a lower dose of edaravone enhanced X-ray-induced apoptosis of some cell lines harboring p53 wild-type status, such as MOLT-4, Nalm-6, and HepG2. The knock-down of p53 using siRNA in MOLT-4 cells abolished the radiosensitizing effect of edaravone. Enhanced phosphorylations of p53 at Ser 15 and Ser 20 and up-regulation of PUMA, a p53 target protein, were observed after X-irradiation in the presence of edaravone. We conclude that the low dose of edaravone sensitized cells to X-irradiation by promoting the p53-dependent apoptotic signaling pathway.","ja":"Edaravone has been reported to have a radioprotective effect at high concentrations. We now report that a lower dose of edaravone enhanced X-ray-induced apoptosis of some cell lines harboring p53 wild-type status, such as MOLT-4, Nalm-6, and HepG2. The knock-down of p53 using siRNA in MOLT-4 cells abolished the radiosensitizing effect of edaravone. Enhanced phosphorylations of p53 at Ser 15 and Ser 20 and up-regulation of PUMA, a p53 target protein, were observed after X-irradiation in the presence of edaravone. We conclude that the low dose of edaravone sensitized cells to X-irradiation by promoting the p53-dependent apoptotic signaling pathway."},"publication_date":"2010-01-25","publication_name":{"en":"Cancer Letters","ja":"Cancer Letters"},"volume":"Vol.293","number":"No.1","starting_page":"52","ending_page":"57","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.canlet.2009.12.020"],"issn":["1872-7980"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:28, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400538"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/20048077","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265053","label":"url"}],"paper_title":{"en":"Sodium orthovanadate inhibits p53-mediated apoptosis.","ja":"Sodium orthovanadate inhibits p53-mediated apoptosis."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Yamamoto Shinichi"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Suzuki Norio"},{"name":"Aoki Shin"},{"name":"Ito Azusa"},{"name":"Nanao Tomohisa"},{"name":"Ohya Soichiro"},{"name":"Yoshino Minako"},{"name":"Zhu Jin"},{"name":"Enomoto Atsushi"},{"name":"Matsumoto Yoshihisa"},{"name":"Funatsu Osamu"},{"name":"Hosoi Yoshio"},{"name":"Ikekita Masahiko"}],"ja":[{"name":"森田 明典"},{"name":"Yamamoto Shinichi"},{"name":"Wang Bing"},{"name":"Tanaka Kaoru"},{"name":"Suzuki Norio"},{"name":"Aoki Shin"},{"name":"Ito Azusa"},{"name":"Nanao Tomohisa"},{"name":"Ohya Soichiro"},{"name":"Yoshino Minako"},{"name":"Zhu Jin"},{"name":"Enomoto Atsushi"},{"name":"Matsumoto Yoshihisa"},{"name":"Funatsu Osamu"},{"name":"Hosoi Yoshio"},{"name":"Ikekita Masahiko"}]},"description":{"en":"Sodium orthovanadate (vanadate) inhibits the DNA-binding activity of p53, but its precise effects on p53 function have not been examined. Here, we show that vanadate exerts a potent antiapoptotic activity through both transcription-dependent and transcription-independent mechanisms relative to other p53 inhibitors, including pifithrin (PFT) alpha. We compared the effects of vanadate to PFTalpha and PFTmicro, an inhibitor of transcription-independent apoptosis by p53. Vanadate suppressed p53-associated apoptotic events at the mitochondria, including the loss of mitochondrial membrane potential, the conformational change of Bax and Bak, the mitochondrial translocation of p53, and the interaction of p53 with Bcl-2. Similarly, vanadate suppressed the apoptosis-inducing activity of a mitochondrially targeted temperature-sensitive p53 in stable transfectants of SaOS-2 cells. In radioprotection assays, which rely on p53, vanadate completely protected mice from a sublethal dose of 8 Gy and partially from a lethal dose of 12 Gy. Together, our findings indicated that vanadate effectively suppresses p53-mediated apoptosis by both transcription-dependent and transcription-independent pathways, and suggested that both pathways must be inhibited to completely block p53-mediated apoptosis.","ja":"Sodium orthovanadate (vanadate) inhibits the DNA-binding activity of p53, but its precise effects on p53 function have not been examined. Here, we show that vanadate exerts a potent antiapoptotic activity through both transcription-dependent and transcription-independent mechanisms relative to other p53 inhibitors, including pifithrin (PFT) alpha. We compared the effects of vanadate to PFTalpha and PFTmicro, an inhibitor of transcription-independent apoptosis by p53. Vanadate suppressed p53-associated apoptotic events at the mitochondria, including the loss of mitochondrial membrane potential, the conformational change of Bax and Bak, the mitochondrial translocation of p53, and the interaction of p53 with Bcl-2. Similarly, vanadate suppressed the apoptosis-inducing activity of a mitochondrially targeted temperature-sensitive p53 in stable transfectants of SaOS-2 cells. In radioprotection assays, which rely on p53, vanadate completely protected mice from a sublethal dose of 8 Gy and partially from a lethal dose of 12 Gy. Together, our findings indicated that vanadate effectively suppresses p53-mediated apoptosis by both transcription-dependent and transcription-independent pathways, and suggested that both pathways must be inhibited to completely block p53-mediated apoptosis."},"publication_date":"2010-01-01","publication_name":{"en":"Cancer Research","ja":"Cancer Research"},"volume":"Vol.70","number":"No.1","starting_page":"257","ending_page":"265","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1158/0008-5472.CAN-08-3771"],"issn":["1538-7445"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:29, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/19733219","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265056","label":"url"}],"paper_title":{"en":"Structural study of the N-glycans of intercellular adhesion molecule-5 (telencephalin).","ja":"Structural study of the N-glycans of intercellular adhesion molecule-5 (telencephalin)."},"authors":{"en":[{"name":"Ohgomori Tomohiro"},{"name":"Funatsu Osamu"},{"name":"Nakaya Syu-ichi"},{"name":"Morita Akinori"},{"name":"Ikekita Masahiko"}],"ja":[{"name":"Ohgomori Tomohiro"},{"name":"Funatsu Osamu"},{"name":"Nakaya Syu-ichi"},{"name":"森田 明典"},{"name":"Ikekita Masahiko"}]},"description":{"en":"Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized membrane glycoprotein expressed in tissues distinct from those expressing other ICAMs. Here, we determined the N-glycan structure of ICAM-5 purified from adult rat brain and compared it with that of other ICAMs. N-glycans were released by N-glycosidase F digestion and labeled with p-amino benzoic octylester (ABOE). ABOE-labeled glycans were analyzed by high performance liquid chromatography (HPLC) and mass spectrometry. The N-glycans obtained from rat brain ICAM-5 consisted of approximately 85% neutral, 10.2% sialylated-only, 2.8% sulfated-only, and 1.2% sialylated and sulfated glycans. Compared with the N-glycan structures of human ICAM-1 expressed in CHO cells, HEK cells, or mouse myeloma cells and ICAM-3 isolated from human T-cells, rat brain ICAM-5 had less highly branched glycans, sialylated glycans, and N-acetyllactosamine structures. In contrast, high-mannose-type N-glycans and Lewis X were more commonly found in rat brain ICAM-5 than in human ICAM-1 expressed in CHO cells, HEK cells, or mouse myeloma cells and ICAM-3 isolated from human T-cells. In addition, sulfated glycans contained GlcNAc 6-O-sulfate on the non-reducing terminal side. Our data will be important for the elucidation of the roles of the N-glycans expressed in neural cells, including those present on ICAM-5.","ja":"Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized membrane glycoprotein expressed in tissues distinct from those expressing other ICAMs. Here, we determined the N-glycan structure of ICAM-5 purified from adult rat brain and compared it with that of other ICAMs. N-glycans were released by N-glycosidase F digestion and labeled with p-amino benzoic octylester (ABOE). ABOE-labeled glycans were analyzed by high performance liquid chromatography (HPLC) and mass spectrometry. The N-glycans obtained from rat brain ICAM-5 consisted of approximately 85% neutral, 10.2% sialylated-only, 2.8% sulfated-only, and 1.2% sialylated and sulfated glycans. Compared with the N-glycan structures of human ICAM-1 expressed in CHO cells, HEK cells, or mouse myeloma cells and ICAM-3 isolated from human T-cells, rat brain ICAM-5 had less highly branched glycans, sialylated glycans, and N-acetyllactosamine structures. In contrast, high-mannose-type N-glycans and Lewis X were more commonly found in rat brain ICAM-5 than in human ICAM-1 expressed in CHO cells, HEK cells, or mouse myeloma cells and ICAM-3 isolated from human T-cells. In addition, sulfated glycans contained GlcNAc 6-O-sulfate on the non-reducing terminal side. Our data will be important for the elucidation of the roles of the N-glycans expressed in neural cells, including those present on ICAM-5."},"publication_date":"2009-09-03","publication_name":{"en":"Biochimica et Biophysica Acta (BBA) - General Subjects","ja":"Biochimica et Biophysica Acta (BBA) - General Subjects"},"volume":"Vol.1790","number":"No.12","starting_page":"1611","ending_page":"1623","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbagen.2009.08.012"],"issn":["0304-4165"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:30, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400539"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/18338353","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265058","label":"url"}],"paper_title":{"en":"BODIPY-based fluorescent redox potential sensors that utilize reversible redox properties of flavin.","ja":"BODIPY-based fluorescent redox potential sensors that utilize reversible redox properties of flavin."},"authors":{"en":[{"name":"Yamada Yasuyuki"},{"name":"Tomiyama Yumiko"},{"name":"Morita Akinori"},{"name":"Ikekita Masahiko"},{"name":"Aoki Shin"}],"ja":[{"name":"Yamada Yasuyuki"},{"name":"Tomiyama Yumiko"},{"name":"森田 明典"},{"name":"Ikekita Masahiko"},{"name":"Aoki Shin"}]},"publication_date":"2008-04-14","publication_name":{"en":"ChemBioChem","ja":"ChemBioChem"},"volume":"Vol.9","number":"No.6","starting_page":"853","ending_page":"856","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1002/cbic.200700718"],"issn":["1439-7633"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:31, {"insert":{"user_id":"6000005112","type":"published_papers","id":"30400540"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/18375133","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265057","label":"url"}],"paper_title":{"en":"Syntheses and applications of fluorescent and biotinylated epolactaene derivatives: Epolactaene and its derivative induce disulfide formation.","ja":"Syntheses and applications of fluorescent and biotinylated epolactaene derivatives: Epolactaene and its derivative induce disulfide formation."},"authors":{"en":[{"name":"Kuramochi Kouji"},{"name":"Yukizawa Shunsuke"},{"name":"Ikeda Seiki"},{"name":"Sunoki Takashi"},{"name":"Arai Satoshi"},{"name":"Matsui Rie"},{"name":"Morita Akinori"},{"name":"Mizushina Yoshiyuki"},{"name":"Sakaguchi Kengo"},{"name":"Sugawara Fumio"},{"name":"Ikekita Masahiko"},{"name":"Kobayashi Susumu"}],"ja":[{"name":"Kuramochi Kouji"},{"name":"Yukizawa Shunsuke"},{"name":"Ikeda Seiki"},{"name":"Sunoki Takashi"},{"name":"Arai Satoshi"},{"name":"Matsui Rie"},{"name":"森田 明典"},{"name":"Mizushina Yoshiyuki"},{"name":"Sakaguchi Kengo"},{"name":"Sugawara Fumio"},{"name":"Ikekita Masahiko"},{"name":"Kobayashi Susumu"}]},"description":{"en":"Epolactaene, isolated from cultured Penicillium sp. BM 1689-P mycelium, induces neurite outgrowth and arrests the cell cycle of the human neuroblastoma cell line, SH-SY5Y, at the G1 phase. We have found that epolactaene and its derivatives induce apoptosis in the human leukemia B-cell line, BALL-1. In this study, we prepared fluorescent and biotinylated epolactaene derivatives. We characterized the cellular location and the identification of BALL-1 proteins that reacted with these compounds. The results obtained from the reaction of epolactaene or its derivative with N-acetylcysteine methyl ester indicate that these compounds induce the disulfide formation and the alpha-position of the epoxylactam core is the reactive site.","ja":"Epolactaene, isolated from cultured Penicillium sp. BM 1689-P mycelium, induces neurite outgrowth and arrests the cell cycle of the human neuroblastoma cell line, SH-SY5Y, at the G1 phase. We have found that epolactaene and its derivatives induce apoptosis in the human leukemia B-cell line, BALL-1. In this study, we prepared fluorescent and biotinylated epolactaene derivatives. We characterized the cellular location and the identification of BALL-1 proteins that reacted with these compounds. The results obtained from the reaction of epolactaene or its derivative with N-acetylcysteine methyl ester indicate that these compounds induce the disulfide formation and the alpha-position of the epoxylactam core is the reactive site."},"publication_date":"2008-03-14","publication_name":{"en":"Bioorganic & Medicinal Chemistry","ja":"Bioorganic & Medicinal Chemistry"},"volume":"Vol.16","number":"No.9","starting_page":"5039","ending_page":"5049","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bmc.2008.03.029"],"issn":["1464-3391"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:32, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/17906693","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265106","label":"url"}],"paper_title":{"en":"Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38).","ja":"Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38)."},"authors":{"en":[{"name":"Enomoto A"},{"name":"Kido N"},{"name":"Ito M"},{"name":"Morita Akinori"},{"name":"Matsumoto Y"},{"name":"Takamatsu N"},{"name":"Hosoi Y"},{"name":"Miyagawa K"}],"ja":[{"name":"Enomoto A"},{"name":"Kido N"},{"name":"Ito M"},{"name":"森田 明典"},{"name":"Matsumoto Y"},{"name":"Takamatsu N"},{"name":"Hosoi Y"},{"name":"Miyagawa K"}]},"description":{"en":"Mitogen-activated protein kinases (MAPKs) are activated through the kinase cascades of MAPK, MAPK kinase (MAPKK) and MAPKK kinase (MAPKKK). MAPKKKs phosphorylate and activate their downstream MAPKKs, which in turn phosphorylate and activate their downstream MAPKs. MAPKKK proteins relay upstream signals through the MAPK cascades to induce cellular responses. However, the molecular mechanisms by which given MAPKKKs are regulated remain largely unknown. Here, we found that serine-threonine protein kinase 38, STK38, physically interacts with the MAPKKKs MEKK1 and MEKK2 (MEKK1/2). The carboxy terminus, including the catalytic domain, but not the amino terminus of MEKK1/2 was necessary for the interaction with STK38. STK38 inhibited MEKK1/2 activation without preventing MEKK1/2 binding to its substrate, SEK1. Importantly, STK38 suppressed the autophosphorylation of MEKK2 without interfering with MEKK2 dimer formation, and converted MEKK2 from its phosphorylated to its nonphosphorylated form. The negative regulation of MEKK1/2 was not due to its phosphorylation by STK38. On the other hand, stk38 short hairpin RNA enhanced sorbitol-induced activation of MEKK2 and phosphorylation of the downstream MAPKKs, MKK3/6. Taken together, our results indicate that STK38 negatively regulates the activation of MEKK1/2 by direct interaction with the catalytic domain of MEKK1/2, suggesting a novel mechanism of MEKK1/2 regulation.","ja":"Mitogen-activated protein kinases (MAPKs) are activated through the kinase cascades of MAPK, MAPK kinase (MAPKK) and MAPKK kinase (MAPKKK). MAPKKKs phosphorylate and activate their downstream MAPKKs, which in turn phosphorylate and activate their downstream MAPKs. MAPKKK proteins relay upstream signals through the MAPK cascades to induce cellular responses. However, the molecular mechanisms by which given MAPKKKs are regulated remain largely unknown. Here, we found that serine-threonine protein kinase 38, STK38, physically interacts with the MAPKKKs MEKK1 and MEKK2 (MEKK1/2). The carboxy terminus, including the catalytic domain, but not the amino terminus of MEKK1/2 was necessary for the interaction with STK38. STK38 inhibited MEKK1/2 activation without preventing MEKK1/2 binding to its substrate, SEK1. Importantly, STK38 suppressed the autophosphorylation of MEKK2 without interfering with MEKK2 dimer formation, and converted MEKK2 from its phosphorylated to its nonphosphorylated form. The negative regulation of MEKK1/2 was not due to its phosphorylation by STK38. On the other hand, stk38 short hairpin RNA enhanced sorbitol-induced activation of MEKK2 and phosphorylation of the downstream MAPKKs, MKK3/6. Taken together, our results indicate that STK38 negatively regulates the activation of MEKK1/2 by direct interaction with the catalytic domain of MEKK1/2, suggesting a novel mechanism of MEKK1/2 regulation."},"publication_date":"2007-10-01","publication_name":{"en":"Oncogene","ja":"Oncogene"},"volume":"Vol.27","number":"No.13","starting_page":"1930","ending_page":"1938","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1038/sj.onc.1210828"],"issn":["1476-5594"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:33, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/16138109","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265107","label":"url"}],"paper_title":{"en":"Sodium orthovanadate suppresses DNA damage-induced caspase activation and apoptosis by inactivating p53.","ja":"Sodium orthovanadate suppresses DNA damage-induced caspase activation and apoptosis by inactivating p53."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Zhu J"},{"name":"Suzuki N"},{"name":"Enomoto A"},{"name":"Matsumoto Y"},{"name":"Tomita M"},{"name":"Suzuki T"},{"name":"Ohtomo K"},{"name":"Hosoi Y"}],"ja":[{"name":"森田 明典"},{"name":"Zhu J"},{"name":"Suzuki N"},{"name":"Enomoto A"},{"name":"Matsumoto Y"},{"name":"Tomita M"},{"name":"Suzuki T"},{"name":"Ohtomo K"},{"name":"Hosoi Y"}]},"description":{"en":"We previously reported that p42/SETbeta is a substrate for caspase-7 in irradiated MOLT-4 cells, and that treating the cells with sodium orthovanadate (vanadate) inhibits p42/SETbeta's caspase-mediated cleavage. Here, we initially found that the inhibitory effect of vanadate was due to the suppression of caspase activation but not of caspase activity. Further investigations revealed that vanadate suppressed upstream of apoptotic events, such as the loss of mitochondrial membrane potential, the conformational change of Bax, and p53 transactivation, although the accumulation, total phosphorylation, and phosphorylation of six individual sites of p53 were not affected. Importantly, vanadate suppressed p53-dependent apoptosis, but not p53-independent apoptosis. Finally, gel-shift and chromatin immunoprecipitation assays conclusively demonstrated that vanadate inhibits the DNA-binding activity of p53. Vanadate is conventionally used as an inhibitor of protein tyrosine phosphatases (PTPs); however, we recommend that the influence of vanadate not only on PTPs but also on p53 be considered before using it.","ja":"We previously reported that p42/SETbeta is a substrate for caspase-7 in irradiated MOLT-4 cells, and that treating the cells with sodium orthovanadate (vanadate) inhibits p42/SETbeta's caspase-mediated cleavage. Here, we initially found that the inhibitory effect of vanadate was due to the suppression of caspase activation but not of caspase activity. Further investigations revealed that vanadate suppressed upstream of apoptotic events, such as the loss of mitochondrial membrane potential, the conformational change of Bax, and p53 transactivation, although the accumulation, total phosphorylation, and phosphorylation of six individual sites of p53 were not affected. Importantly, vanadate suppressed p53-dependent apoptosis, but not p53-independent apoptosis. Finally, gel-shift and chromatin immunoprecipitation assays conclusively demonstrated that vanadate inhibits the DNA-binding activity of p53. Vanadate is conventionally used as an inhibitor of protein tyrosine phosphatases (PTPs); however, we recommend that the influence of vanadate not only on PTPs but also on p53 be considered before using it."},"publication_date":"2006-03","publication_name":{"en":"Cell Death and Differentiation","ja":"Cell Death and Differentiation"},"volume":"Vol.13","number":"No.3","starting_page":"499","ending_page":"511","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1038/sj.cdd.4401768"],"issn":["1350-9047"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:34, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/16414009","label":"url"},{"@id":"https://www.scopus.com/record/display.url?eid=2-s2.0-31444451032&origin=inward","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265059","label":"url"}],"paper_title":{"en":"Src tyrosine kinase inhibitor PP2 suppresses ERK1/2 activation and epidermal growth factor receptor transactivation by X-irradiation.","ja":"Src tyrosine kinase inhibitor PP2 suppresses ERK1/2 activation and epidermal growth factor receptor transactivation by X-irradiation."},"authors":{"en":[{"name":"Li Zhiping"},{"name":"Hosoi Yoshio"},{"name":"Cai Keshong"},{"name":"Tanno Yuji"},{"name":"Matsumoto Yoshihisa"},{"name":"Enomoto Atsushi"},{"name":"Morita Akinori"},{"name":"Nakagawa Keiichi"},{"name":"Miyagawa Kiyoshi"}],"ja":[{"name":"Li Zhiping"},{"name":"Hosoi Yoshio"},{"name":"Cai Keshong"},{"name":"Tanno Yuji"},{"name":"Matsumoto Yoshihisa"},{"name":"Enomoto Atsushi"},{"name":"森田 明典"},{"name":"Nakagawa Keiichi"},{"name":"Miyagawa Kiyoshi"}]},"description":{"en":"Exposure of MDA-MB-468 cells to ionizing radiation (IR) caused biphasic activation of ERK as indicated by its phosphorylation at Thr202/Tyr204. Specific epidermal growth factor receptor (EGFR) inhibitor AG1478 and specific Src inhibitor PP2 inhibited IR-induced ERK1/2 activation but phosphatidylinositol-3 kinase inhibitor wortmannin did not. IR caused EGFR tyrosine phosphorylation, whereas it did not induce EGFR autophosphorylation at Tyr992, Tyr1045, and Tyr1068 or Src-dependent EGFR phosphorylation at Tyr845. SHP-2, which positively regulates EGFR/Ras/ERK signaling cascade, became activated by IR as indicated by its phosphorylation at Tyr542. This activation was inhibited by PP2 not by AG1478, which suggests Src-dependent activation of SHP-2. Src and PTPalpha, which positively regulates Src, became activated as indicated by phosphorylation at Tyr416 and Tyr789, respectively. These data suggest that IR-induced ERK1/2 activation involves EGFR through a Src-dependent pathway that is distinct from EGFR ligand activation.","ja":"Exposure of MDA-MB-468 cells to ionizing radiation (IR) caused biphasic activation of ERK as indicated by its phosphorylation at Thr202/Tyr204. Specific epidermal growth factor receptor (EGFR) inhibitor AG1478 and specific Src inhibitor PP2 inhibited IR-induced ERK1/2 activation but phosphatidylinositol-3 kinase inhibitor wortmannin did not. IR caused EGFR tyrosine phosphorylation, whereas it did not induce EGFR autophosphorylation at Tyr992, Tyr1045, and Tyr1068 or Src-dependent EGFR phosphorylation at Tyr845. SHP-2, which positively regulates EGFR/Ras/ERK signaling cascade, became activated by IR as indicated by its phosphorylation at Tyr542. This activation was inhibited by PP2 not by AG1478, which suggests Src-dependent activation of SHP-2. Src and PTPalpha, which positively regulates Src, became activated as indicated by phosphorylation at Tyr416 and Tyr789, respectively. These data suggest that IR-induced ERK1/2 activation involves EGFR through a Src-dependent pathway that is distinct from EGFR ligand activation."},"publication_date":"2006-01-18","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.341","number":"No.2","starting_page":"363","ending_page":"368","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbrc.2005.12.193"],"issn":["0006-291X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:35, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15381073","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265062","label":"url"}],"paper_title":{"en":"Potentiality of DNA-dependent protein kinase to phosphorylate Ser46 of human p53.","ja":"Potentiality of DNA-dependent protein kinase to phosphorylate Ser46 of human p53."},"authors":{"en":[{"name":"Komiyama Shingo"},{"name":"Taniguchi Sachiko"},{"name":"Matsumoto Yoshihisa"},{"name":"Tsunoda Eri"},{"name":"Ohto Takayo"},{"name":"Suzuki Yuka"},{"name":"Yin Hong-Lan"},{"name":"Tomita Masanori"},{"name":"Enomoto Atsushi"},{"name":"Morita Akinori"},{"name":"Suzuki Takahiko"},{"name":"Ohtomo Kuni"},{"name":"Hosoi Yoshio"},{"name":"Suzuki Norio"}],"ja":[{"name":"Komiyama Shingo"},{"name":"Taniguchi Sachiko"},{"name":"Matsumoto Yoshihisa"},{"name":"Tsunoda Eri"},{"name":"Ohto Takayo"},{"name":"Suzuki Yuka"},{"name":"Yin Hong-Lan"},{"name":"Tomita Masanori"},{"name":"Enomoto Atsushi"},{"name":"森田 明典"},{"name":"Suzuki Takahiko"},{"name":"Ohtomo Kuni"},{"name":"Hosoi Yoshio"},{"name":"Suzuki Norio"}]},"description":{"en":"DNA damage induces accumulation and activation of p53 via various posttranslational modifications. Among them, several lines of evidence indicated the phosphorylation of Ser46 as an important mediator of DNA damage-induced apoptosis but the responsible kinase remains to be clarified, especially in the case of ionizing radiation (IR). Here we showed that DNA-dependent protein kinase (DNA-PK) could phosphorylate Ser46 of p53 in addition to reported phosphorylation sites Ser15 and Ser37. However, IR-induced phosphorylation of Ser46 was seen even in M059J, a human glioma cell line lacking DNA-PKcs, and it was, at most, only slightly less than in control M059K. On the other hand, a related kinase ataxia-telangiectasia mutated (ATM), which was shown to be essential for IR-induced phosphorylation of Ser46, could poorly phosphorylate Ser46 by itself. These results collectively suggested two pathways for IR-induced phosphorylation of Ser46, i.e., direct phosphorylation by DNA-PK and indirect phosphorylation via ATM.","ja":"DNA damage induces accumulation and activation of p53 via various posttranslational modifications. Among them, several lines of evidence indicated the phosphorylation of Ser46 as an important mediator of DNA damage-induced apoptosis but the responsible kinase remains to be clarified, especially in the case of ionizing radiation (IR). Here we showed that DNA-dependent protein kinase (DNA-PK) could phosphorylate Ser46 of p53 in addition to reported phosphorylation sites Ser15 and Ser37. However, IR-induced phosphorylation of Ser46 was seen even in M059J, a human glioma cell line lacking DNA-PKcs, and it was, at most, only slightly less than in control M059K. On the other hand, a related kinase ataxia-telangiectasia mutated (ATM), which was shown to be essential for IR-induced phosphorylation of Ser46, could poorly phosphorylate Ser46 by itself. These results collectively suggested two pathways for IR-induced phosphorylation of Ser46, i.e., direct phosphorylation by DNA-PK and indirect phosphorylation via ATM."},"publication_date":"2004-10-22","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.323","number":"No.3","starting_page":"816","ending_page":"822","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.bbrc.2004.08.161"],"issn":["0006-291X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:36, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15447039","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265060","label":"url"}],"paper_title":{"en":"Radiosensitization by hyperthermia in the chicken B-lymphocyte cell line DT40 and its derivatives lacking nonhomologous end joining and/or homologous recombination pathways of DNA double-strand break repair.","ja":"Radiosensitization by hyperthermia in the chicken B-lymphocyte cell line DT40 and its derivatives lacking nonhomologous end joining and/or homologous recombination pathways of DNA double-strand break repair."},"authors":{"en":[{"name":"Yin Hong Lan"},{"name":"Suzuki Yuka"},{"name":"Matsumoto Yoshihisa"},{"name":"Tomita Masanori"},{"name":"Furusawa Yoshiya"},{"name":"Enomoto Atsushi"},{"name":"Morita Akinori"},{"name":"Aoki Mizuho"},{"name":"Yatagai Fumio"},{"name":"Suzuki Takahiko"},{"name":"Hosoi Yoshio"},{"name":"Ohtomo Kuni"},{"name":"Suzuki Norio"}],"ja":[{"name":"Yin Hong Lan"},{"name":"Suzuki Yuka"},{"name":"Matsumoto Yoshihisa"},{"name":"Tomita Masanori"},{"name":"古澤 佳也"},{"name":"Enomoto Atsushi"},{"name":"森田 明典"},{"name":"Aoki Mizuho"},{"name":"Yatagai Fumio"},{"name":"Suzuki Takahiko"},{"name":"Hosoi Yoshio"},{"name":"Ohtomo Kuni"},{"name":"Suzuki Norio"}]},"description":{"en":"Hyperthermia has a radiosensitizing effect, which is one of the most important biological bases for its use in cancer therapy with radiation. Although the mechanism of this effect has not been clarified in molecular terms, possible involvement of either one or both of two major DNA double-strand break (DSB) repair pathways, i.e. nonhomologous end joining (NHEJ) and homologous recombination (HR), has been speculated. To test this possibility, we examined cells of the chicken B-lymphocyte cell line DT40 and its derivatives lacking NHEJ and/or HR: KU70(-/-), DNA-PKcs(-/-/-), RAD54(-/-) and KU70(-/-)/RAD54(-/-). Radiosensitization by hyperthermia could be seen in all of the mutants, including KU70(-/-)/RAD54(-/-), which lacked both NHEJ and HR. Therefore, radiosensitization by hyperthermia cannot be explained simply by its inhibitory effects, if any, on NHEJ and/or HR alone. However, in NHEJ-defective KU70(-/-) and DNA-PKcs(-/-/-), consisting of two subpopulations with distinct radiosensitivity, the radiosensitive subpopulation, which is considered to be cells in G(1) and early S, was not sensitized. Substantial sensitization was seen only in the radioresistant subpopulation, which is considered to be cells in late S and G(2), capable of repairing DSBs through HR. This observation did not exclude possible involvement of NHEJ in G(1) and early S phase and also suggested inhibitory effects of hyperthermia on HR. Thus partial contribution of NHEJ and HR in radiosensitization by hyperthermia, especially that depending on the cell cycle stage, remains to be considered.","ja":"Hyperthermia has a radiosensitizing effect, which is one of the most important biological bases for its use in cancer therapy with radiation. Although the mechanism of this effect has not been clarified in molecular terms, possible involvement of either one or both of two major DNA double-strand break (DSB) repair pathways, i.e. nonhomologous end joining (NHEJ) and homologous recombination (HR), has been speculated. To test this possibility, we examined cells of the chicken B-lymphocyte cell line DT40 and its derivatives lacking NHEJ and/or HR: KU70(-/-), DNA-PKcs(-/-/-), RAD54(-/-) and KU70(-/-)/RAD54(-/-). Radiosensitization by hyperthermia could be seen in all of the mutants, including KU70(-/-)/RAD54(-/-), which lacked both NHEJ and HR. Therefore, radiosensitization by hyperthermia cannot be explained simply by its inhibitory effects, if any, on NHEJ and/or HR alone. However, in NHEJ-defective KU70(-/-) and DNA-PKcs(-/-/-), consisting of two subpopulations with distinct radiosensitivity, the radiosensitive subpopulation, which is considered to be cells in G(1) and early S, was not sensitized. Substantial sensitization was seen only in the radioresistant subpopulation, which is considered to be cells in late S and G(2), capable of repairing DSBs through HR. This observation did not exclude possible involvement of NHEJ in G(1) and early S phase and also suggested inhibitory effects of hyperthermia on HR. Thus partial contribution of NHEJ and HR in radiosensitization by hyperthermia, especially that depending on the cell cycle stage, remains to be considered."},"publication_date":"2004-10","publication_name":{"en":"Radiation Research","ja":"Radiation Research"},"volume":"Vol.162","number":"No.4","starting_page":"433","ending_page":"441","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1667/RR3239"],"issn":["0033-7587"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:37, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15378840","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265063","label":"url"}],"paper_title":{"en":"Suramin Sensitizes cells to ionizing radiation by inactivating DNA-dependent protein kinase.","ja":"Suramin Sensitizes cells to ionizing radiation by inactivating DNA-dependent protein kinase."},"authors":{"en":[{"name":"Hosoi Yoshio"},{"name":"Matsumoto Yoshihisa"},{"name":"Enomoto Atsushi"},{"name":"Morita Akinori"},{"name":"Green Joseph"},{"name":"Nakagawa Keiichi"},{"name":"Naruse Kiyoshi"},{"name":"Suzuki Norio"}],"ja":[{"name":"Hosoi Yoshio"},{"name":"Matsumoto Yoshihisa"},{"name":"Enomoto Atsushi"},{"name":"森田 明典"},{"name":"Green Joseph"},{"name":"Nakagawa Keiichi"},{"name":"Naruse Kiyoshi"},{"name":"Suzuki Norio"}]},"description":{"en":"Here we report that suramin sensitizes LM217, MDA-MB-468, T98G and A431 cells to ionizing radiation. Suramin sensitized cells to X radiation in a dose-dependent fashion, and longer exposure to suramin before X irradiation resulted in more efficient sensitization. The dose-modifying factors calculated from the survival curves were 1.18 in LM217 cells and 1.37 in MDA-MB-468 cells. Suramin did not sensitize Scid cells that had no DNA-dependent protein kinase activity. Suramin inhibited DNA-dependent protein kinase activity in vitro and in vivo. The concentration of suramin resulting in 50% inhibition in vitro was 1.7 microM in LM217 cells and 2.4 microM in MDA-MB-468 cells. Exposure of LM217 and MDA-MB-468 cells to suramin did not affect the level of Ku70 (G22P1) or Ku80 (XRCC5), but it increased the level of DNA-PKcs(PRKDC). Suramin did not sensitize LM217 or MDA-MB-468 cells to UV radiation. Suramin's effects were not caused by accumulation of cells in a specific phase of the cell cycle. These results suggest that suramin sensitizes cells to ionizing radiation by inhibiting DNA-dependent protein kinase activity.","ja":"Here we report that suramin sensitizes LM217, MDA-MB-468, T98G and A431 cells to ionizing radiation. Suramin sensitized cells to X radiation in a dose-dependent fashion, and longer exposure to suramin before X irradiation resulted in more efficient sensitization. The dose-modifying factors calculated from the survival curves were 1.18 in LM217 cells and 1.37 in MDA-MB-468 cells. Suramin did not sensitize Scid cells that had no DNA-dependent protein kinase activity. Suramin inhibited DNA-dependent protein kinase activity in vitro and in vivo. The concentration of suramin resulting in 50% inhibition in vitro was 1.7 microM in LM217 cells and 2.4 microM in MDA-MB-468 cells. Exposure of LM217 and MDA-MB-468 cells to suramin did not affect the level of Ku70 (G22P1) or Ku80 (XRCC5), but it increased the level of DNA-PKcs(PRKDC). Suramin did not sensitize LM217 or MDA-MB-468 cells to UV radiation. Suramin's effects were not caused by accumulation of cells in a specific phase of the cell cycle. These results suggest that suramin sensitizes cells to ionizing radiation by inhibiting DNA-dependent protein kinase activity."},"publication_date":"2004-09","publication_name":{"en":"Radiation Research","ja":"Radiation Research"},"volume":"Vol.162","number":"No.3","starting_page":"308","ending_page":"314","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1667/RR3217"],"issn":["0033-7587"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:38, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/15254745","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265064","label":"url"}],"paper_title":{"en":"Up-regulation of DNA-dependent protein kinase activity and Sp1 in colorectal cancer.","ja":"Up-regulation of DNA-dependent protein kinase activity and Sp1 in colorectal cancer."},"authors":{"en":[{"name":"Hosoi Yoshio"},{"name":"Watanabe Toshiaki"},{"name":"Nakagawa Keiichi"},{"name":"Matsumoto Yoshihisa"},{"name":"Enomoto Atsushi"},{"name":"Morita Akinori"},{"name":"Nagawa Hirokazu"},{"name":"Suzuki Norio"}],"ja":[{"name":"Hosoi Yoshio"},{"name":"Watanabe Toshiaki"},{"name":"Nakagawa Keiichi"},{"name":"Matsumoto Yoshihisa"},{"name":"Enomoto Atsushi"},{"name":"森田 明典"},{"name":"Nagawa Hirokazu"},{"name":"Suzuki Norio"}]},"description":{"en":"Tumor tissues and adjacent normal tissues in 12 colorectal cancers were examined for quantitative differences in: i) activity of DNA-dependent protein kinase (DNA-PK), which functions in DNA double-strand breads repair, and ii) protein and mRNA levels of Ku70, Ku80, DNA-PKcs and transcriptional factor Sp1. DNA-PK activity and protein/mRNA levels of Ku70, Ku80, DNA-PKcs and Sp1 were significantly higher in the tumor tissues compared with the normal tissues. Significant correlations between DNA-PK activity and protein/mRNA levels of Ku70, Ku80, DNA-PKcs and Sp1 were observed. Because Ku80 and DNA-PKcs have consensus Sp1 recognition elements in their promoter region, the DNA sequence of Ku70 promoter region was analyzed. Analysis of Ku70 promoter region reveled that Ku70 gene has consensus Sp1 recognition elements in its promoter region. mRNA levels of Ku70, Ku80 and DNA-PKcs were correlated with one another, and significant correlations between Sp1 protein level and mRNA levels of Ku70 and Ku80 were observed. These results suggest that DNA-PK activity and protein- and mRNA-levels of Ku70, Ku80 and DNA-PKcs were elevated in tumor tissues in patients with colorectal cancer because of elevated Sp1 protein levels in tumor tissues.","ja":"Tumor tissues and adjacent normal tissues in 12 colorectal cancers were examined for quantitative differences in: i) activity of DNA-dependent protein kinase (DNA-PK), which functions in DNA double-strand breads repair, and ii) protein and mRNA levels of Ku70, Ku80, DNA-PKcs and transcriptional factor Sp1. DNA-PK activity and protein/mRNA levels of Ku70, Ku80, DNA-PKcs and Sp1 were significantly higher in the tumor tissues compared with the normal tissues. Significant correlations between DNA-PK activity and protein/mRNA levels of Ku70, Ku80, DNA-PKcs and Sp1 were observed. Because Ku80 and DNA-PKcs have consensus Sp1 recognition elements in their promoter region, the DNA sequence of Ku70 promoter region was analyzed. Analysis of Ku70 promoter region reveled that Ku70 gene has consensus Sp1 recognition elements in its promoter region. mRNA levels of Ku70, Ku80 and DNA-PKcs were correlated with one another, and significant correlations between Sp1 protein level and mRNA levels of Ku70 and Ku80 were observed. These results suggest that DNA-PK activity and protein- and mRNA-levels of Ku70, Ku80 and DNA-PKcs were elevated in tumor tissues in patients with colorectal cancer because of elevated Sp1 protein levels in tumor tissues."},"publication_date":"2004-08","publication_name":{"en":"International Journal of Oncology","ja":"International Journal of Oncology"},"volume":"Vol.25","number":"No.2","starting_page":"461","ending_page":"468","languages":["eng"],"referee":true,"identifiers":{"issn":["1019-6439"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:39, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/14555350","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265103","label":"url"}],"paper_title":{"en":"Difference in the heat sensitivity of DNA-dependent protein kinase activity among mouse, hamster and human cells.","ja":"Difference in the heat sensitivity of DNA-dependent protein kinase activity among mouse, hamster and human cells."},"authors":{"en":[{"name":"Umeda N"},{"name":"Matsumoto Y"},{"name":"Yin H-L"},{"name":"Tomita M"},{"name":"Enomoto A"},{"name":"Morita Akinori"},{"name":"Mizukoshi T"},{"name":"Sakai K"},{"name":"Hosoi Y"},{"name":"Suzuki N"}],"ja":[{"name":"Umeda N"},{"name":"Matsumoto Y"},{"name":"Yin H-L"},{"name":"Tomita M"},{"name":"Enomoto A"},{"name":"森田 明典"},{"name":"Mizukoshi T"},{"name":"Sakai K"},{"name":"Hosoi Y"},{"name":"Suzuki N"}]},"description":{"en":"The heat sensitivity of DNA-PK was clearly different among mouse, hamster and human cells. The results suggested a possibility that the role of DNA-PK inactivation in hyperthermic radiosensitization might be variable, depending on cells, and would reinforce the warning that the direct extrapolation of data from rodent cells might lead to overestimation of the effectiveness of hyperthermia on human cancer.","ja":"The heat sensitivity of DNA-PK was clearly different among mouse, hamster and human cells. The results suggested a possibility that the role of DNA-PK inactivation in hyperthermic radiosensitization might be variable, depending on cells, and would reinforce the warning that the direct extrapolation of data from rodent cells might lead to overestimation of the effectiveness of hyperthermia on human cancer."},"publication_date":"2003-08","publication_name":{"en":"International Journal of Radiation Biology","ja":"International Journal of Radiation Biology"},"volume":"Vol.79","number":"No.8","starting_page":"671","ending_page":"680","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1080/09553000310001596959"],"issn":["0955-3002"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:40, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/14555342","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265101","label":"url"}],"paper_title":{"en":"Decreased c-Myc expression and its involvement in X-ray-induced apoptotic cell death of human T-cell leukaemia cell line MOLT-4.","ja":"Decreased c-Myc expression and its involvement in X-ray-induced apoptotic cell death of human T-cell leukaemia cell line MOLT-4."},"authors":{"en":[{"name":"Enomoto A"},{"name":"Suzuki N"},{"name":"Kang Y"},{"name":"Hirano K"},{"name":"Matsumoto Y"},{"name":"Zhu J"},{"name":"Morita Akinori"},{"name":"Hosoi Y"},{"name":"Sakai K"},{"name":"Koyama H"}],"ja":[{"name":"Enomoto A"},{"name":"Suzuki N"},{"name":"Kang Y"},{"name":"Hirano K"},{"name":"Matsumoto Y"},{"name":"Zhu J"},{"name":"森田 明典"},{"name":"Hosoi Y"},{"name":"Sakai K"},{"name":"Koyama H"}]},"description":{"en":"A decrease of c-Myc protein was considered important in X-ray-induced apoptotic cell death of MOLT-4 cells; activation of the JNK pathway caused reduction in the amounts of c-myc mRNA and c-Myc protein, and finally induced apoptotic cell death.","ja":"A decrease of c-Myc protein was considered important in X-ray-induced apoptotic cell death of MOLT-4 cells; activation of the JNK pathway caused reduction in the amounts of c-myc mRNA and c-Myc protein, and finally induced apoptotic cell death."},"publication_date":"2003-08","publication_name":{"en":"International Journal of Radiation Biology","ja":"International Journal of Radiation Biology"},"volume":"Vol.79","number":"No.8","starting_page":"589","ending_page":"600","languages":["eng"],"referee":true,"identifiers":{"issn":["0955-3002"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:41, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/12821118","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265065","label":"url"}],"paper_title":{"en":"Caspase-mediated cleavage of JNK during stress-induced apoptosis.","ja":"Caspase-mediated cleavage of JNK during stress-induced apoptosis."},"authors":{"en":[{"name":"Enomoto Atsushi"},{"name":"Suzuki Norio"},{"name":"Morita Akinori"},{"name":"Ito Michihiko"},{"name":"Liu Chang Qing"},{"name":"Matsumoto Yoshihisa"},{"name":"Yoshioka Katsuji"},{"name":"Shiba Tadayoshi"},{"name":"Hosoi Yoshio"}],"ja":[{"name":"Enomoto Atsushi"},{"name":"Suzuki Norio"},{"name":"森田 明典"},{"name":"Ito Michihiko"},{"name":"Liu Chang Qing"},{"name":"Matsumoto Yoshihisa"},{"name":"Yoshioka Katsuji"},{"name":"Shiba Tadayoshi"},{"name":"Hosoi Yoshio"}]},"description":{"en":"The c-Jun N-terminal kinases (JNKs) are a subfamily of the mitogen-activated protein kinases (MAPKs). The JNKs are encoded by three separate genes (jnk1, jnk2, and jnk3), which are spliced alternatively to create 10 JNK isoforms that are either p46 or p54 in size. In this study, we found that the p52 form of JNK emerged in human leukemia MOLT-4 or U937 cells following X-irradiation or heat treatment. The accumulation of p52 coincided with the reduction of p54 JNK. On the other hand, the amounts of p46 JNK did not change by X-irradiation. Induction of the p52 form of JNK also paralleled the appearance of the active form of caspase-3 and was suppressed by a caspase-specific inhibitor, Ac-DEVD-CHO, but not by Ac-YVAD-CHO. In vitro cleavage assays indicated that recombinant human JNK1beta2 and JNK2beta2 were cleaved by caspase-3, and that the mutation of aspartic acid at position 413 of JNK1beta2 or 410 of JNK2beta2 to alanine abolished the cleavage. Altogether, our results demonstrated that p54 JNKs, at least JNK1beta2 and JNK2beta2, were new selective targets of caspases in JNK splicing variants, and suggested that the p52 form could serve as a marker of apoptosis.","ja":"The c-Jun N-terminal kinases (JNKs) are a subfamily of the mitogen-activated protein kinases (MAPKs). The JNKs are encoded by three separate genes (jnk1, jnk2, and jnk3), which are spliced alternatively to create 10 JNK isoforms that are either p46 or p54 in size. In this study, we found that the p52 form of JNK emerged in human leukemia MOLT-4 or U937 cells following X-irradiation or heat treatment. The accumulation of p52 coincided with the reduction of p54 JNK. On the other hand, the amounts of p46 JNK did not change by X-irradiation. Induction of the p52 form of JNK also paralleled the appearance of the active form of caspase-3 and was suppressed by a caspase-specific inhibitor, Ac-DEVD-CHO, but not by Ac-YVAD-CHO. In vitro cleavage assays indicated that recombinant human JNK1beta2 and JNK2beta2 were cleaved by caspase-3, and that the mutation of aspartic acid at position 413 of JNK1beta2 or 410 of JNK2beta2 to alanine abolished the cleavage. Altogether, our results demonstrated that p54 JNKs, at least JNK1beta2 and JNK2beta2, were new selective targets of caspases in JNK splicing variants, and suggested that the p52 form could serve as a marker of apoptosis."},"publication_date":"2003-07-11","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.306","number":"No.4","starting_page":"837","ending_page":"842","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/S0006-291X(03)01050-7"],"issn":["0006-291X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:42, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/11953863","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265104","label":"url"}],"paper_title":{"en":"Phosphorothioate oligonucleotides, suramin and heparin inhibit DNA-dependent protein kinase activity.","ja":"Phosphorothioate oligonucleotides, suramin and heparin inhibit DNA-dependent protein kinase activity."},"authors":{"en":[{"name":"Hosoi Y"},{"name":"Matsumoto Y"},{"name":"Tomita M"},{"name":"Enomoto A"},{"name":"Morita Akinori"},{"name":"Sakai K"},{"name":"Umeda N"},{"name":"Zhao H-J"},{"name":"Nakagawa K"},{"name":"Ono T"},{"name":"Suzuki N"}],"ja":[{"name":"Hosoi Y"},{"name":"Matsumoto Y"},{"name":"Tomita M"},{"name":"Enomoto A"},{"name":"森田 明典"},{"name":"Sakai K"},{"name":"Umeda N"},{"name":"Zhao H-J"},{"name":"Nakagawa K"},{"name":"Ono T"},{"name":"Suzuki N"}]},"description":{"en":"Phosphorothioate oligonucleotides and suramin bind to heparin binding proteins including DNA polymerases, and inhibit their functions. In the present study, we report inhibition of DNA-dependent protein kinase activity by phosphorothioate oligonucleotides, suramin and heparin. Inhibitory effect of phosphorothioate oligonucleotides on DNA-dependent protein kinase activity was increased with length and reached a plateau at 36-mer. The base composition of phosphorothioate oligonucleotides did not affect the inhibitory effect. The inhibitory effect by phosphorothioate oligodeoxycytidine 36-mer can be about 200-fold greater than that by the phosphodiester oligodeoxycytidine 36-mer. The inhibitory effect was also observed with purified DNA-dependent protein kinase, which suggests direct interaction between DNA-dependent protein kinase and phosphorothioate oligonucleotides. DNA-dependent protein kinase will have different binding positions for double-stranded DNA and phosphorothioate oligodeoxycytidine 36-mer because they were not competitive in DNA-dependent protein kinase activation. Suramin and heparin inhibited DNA-dependent protein kinase activity with IC(50) of 1.7 microM and 0.27 microg ml(-1) respectively. DNA-dependent protein kinase activities and DNA double-stranded breaks repair in cultured cells were significantly suppressed by the treatment with suramin in vivo. Our present observations suggest that suramin may possibly result in sensitisation of cells to ionising radiation by inactivation of DNA-dependent protein kinase and the impairment of double-stranded breaks repair.","ja":"Phosphorothioate oligonucleotides and suramin bind to heparin binding proteins including DNA polymerases, and inhibit their functions. In the present study, we report inhibition of DNA-dependent protein kinase activity by phosphorothioate oligonucleotides, suramin and heparin. Inhibitory effect of phosphorothioate oligonucleotides on DNA-dependent protein kinase activity was increased with length and reached a plateau at 36-mer. The base composition of phosphorothioate oligonucleotides did not affect the inhibitory effect. The inhibitory effect by phosphorothioate oligodeoxycytidine 36-mer can be about 200-fold greater than that by the phosphodiester oligodeoxycytidine 36-mer. The inhibitory effect was also observed with purified DNA-dependent protein kinase, which suggests direct interaction between DNA-dependent protein kinase and phosphorothioate oligonucleotides. DNA-dependent protein kinase will have different binding positions for double-stranded DNA and phosphorothioate oligodeoxycytidine 36-mer because they were not competitive in DNA-dependent protein kinase activation. Suramin and heparin inhibited DNA-dependent protein kinase activity with IC(50) of 1.7 microM and 0.27 microg ml(-1) respectively. DNA-dependent protein kinase activities and DNA double-stranded breaks repair in cultured cells were significantly suppressed by the treatment with suramin in vivo. Our present observations suggest that suramin may possibly result in sensitisation of cells to ionising radiation by inactivation of DNA-dependent protein kinase and the impairment of double-stranded breaks repair."},"publication_date":"2002-04-08","publication_name":{"en":"British Journal of Cancer","ja":"British Journal of Cancer"},"volume":"Vol.86","number":"No.7","starting_page":"1143","ending_page":"1149","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1038/sj.bjc.6600191"],"issn":["0007-0920"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:43, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/11571020","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265102","label":"url"}],"paper_title":{"en":"Involvement of c-Jun NH2-terminal kinase-1 in heat-induced apoptotic cell death of human monoblastic leukaemia U937 cells.","ja":"Involvement of c-Jun NH2-terminal kinase-1 in heat-induced apoptotic cell death of human monoblastic leukaemia U937 cells."},"authors":{"en":[{"name":"Enomoto A"},{"name":"Suzuki N"},{"name":"Liu C"},{"name":"Kang Y"},{"name":"Zhu J"},{"name":"Serizawa S"},{"name":"Matsumoto Y"},{"name":"Morita Akinori"},{"name":"Ito M"},{"name":"Hosoi Y"}],"ja":[{"name":"Enomoto A"},{"name":"Suzuki N"},{"name":"Liu C"},{"name":"Kang Y"},{"name":"Zhu J"},{"name":"Serizawa S"},{"name":"Matsumoto Y"},{"name":"森田 明典"},{"name":"Ito M"},{"name":"Hosoi Y"}]},"description":{"en":"Prolonged phosphorylation or activation of JNK1 was considered important for heat-induced apoptosis and JNK1 may control the process possibly through phosphorylation of HSP27 and caspase-9 activation in U937 cells.","ja":"Prolonged phosphorylation or activation of JNK1 was considered important for heat-induced apoptosis and JNK1 may control the process possibly through phosphorylation of HSP27 and caspase-9 activation in U937 cells."},"publication_date":"2001-08","publication_name":{"en":"International Journal of Radiation Biology","ja":"International Journal of Radiation Biology"},"volume":"Vol.77","number":"No.8","starting_page":"867","ending_page":"874","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1080/09553000110062512"],"issn":["0955-3002"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:44, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/11095960","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265099","label":"url"}],"paper_title":{"en":"p41 as a possible marker for cell death is generated by caspase cleavage of p42/SETbeta in irradiated MOLT-4 cells.","ja":"p41 as a possible marker for cell death is generated by caspase cleavage of p42/SETbeta in irradiated MOLT-4 cells."},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Suzuki N"},{"name":"Matsumoto Y"},{"name":"Hirano K"},{"name":"Enomoto A"},{"name":"Zhu J"},{"name":"Sakai K"}],"ja":[{"name":"森田 明典"},{"name":"Suzuki N"},{"name":"Matsumoto Y"},{"name":"Hirano K"},{"name":"Enomoto A"},{"name":"Zhu J"},{"name":"Sakai K"}]},"description":{"en":"We have reported previously that X-irradiated MOLT-4 cells during their rapid cell death exhibited dose and time dependently a new protein named p41 detected by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). An antibody, AM-1, raised against partial peptide of p41 stained two spots, p41 and p42, unexpectedly. Amino acid sequence analysis of partial peptides showed homology between p41 and a putative oncogene, set. In the present study, N-terminal amino acid sequencing of p41 and p42, and polyclonal antibodies newly prepared against different partial peptide sequences revealed that p41 was a N-terminal truncation form of p42, and p42 was identified as SETbeta. The cleavage site was at carboxyl end of SNHD 18 of p42. Radiation-induced p42 cleavage as well as apoptotic cell death was suppressed by a caspase-specific inhibitor Ac-DEVD-CHO but not by Ac-YVAD-CHO. Further in vitro cleavage experiments with recombinant p42 and either irradiated cell extracts or recombinant caspases concluded that the cleavage of p42 into p41 was catalyzed by caspase(s) mainly by caspase-7. One of newly raised antibodies, AM-4, specific to p41 or specific to cleavage site of p42, was found useful enabling simple detection of p41 by 1-D PAGE instead of laborious 2-D PAGE. p41 may serve as a marker of apoptotic cell death.","ja":"We have reported previously that X-irradiated MOLT-4 cells during their rapid cell death exhibited dose and time dependently a new protein named p41 detected by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). An antibody, AM-1, raised against partial peptide of p41 stained two spots, p41 and p42, unexpectedly. Amino acid sequence analysis of partial peptides showed homology between p41 and a putative oncogene, set. In the present study, N-terminal amino acid sequencing of p41 and p42, and polyclonal antibodies newly prepared against different partial peptide sequences revealed that p41 was a N-terminal truncation form of p42, and p42 was identified as SETbeta. The cleavage site was at carboxyl end of SNHD 18 of p42. Radiation-induced p42 cleavage as well as apoptotic cell death was suppressed by a caspase-specific inhibitor Ac-DEVD-CHO but not by Ac-YVAD-CHO. Further in vitro cleavage experiments with recombinant p42 and either irradiated cell extracts or recombinant caspases concluded that the cleavage of p42 into p41 was catalyzed by caspase(s) mainly by caspase-7. One of newly raised antibodies, AM-4, specific to p41 or specific to cleavage site of p42, was found useful enabling simple detection of p41 by 1-D PAGE instead of laborious 2-D PAGE. p41 may serve as a marker of apoptotic cell death."},"publication_date":"2000-11-30","publication_name":{"en":"Biochemical and Biophysical Research Communications","ja":"Biochemical and Biophysical Research Communications"},"volume":"Vol.278","number":"No.3","starting_page":"627","ending_page":"632","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1006/bbrc.2000.3860"],"issn":["0006-291X"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:45, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10822128","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265098","label":"url"}],"paper_title":{"en":"Involvement of SAPK/JNK pathway in X-ray-induced rapid cell death of human T-cell leukemia cell line MOLT-4.","ja":"Involvement of SAPK/JNK pathway in X-ray-induced rapid cell death of human T-cell leukemia cell line MOLT-4."},"authors":{"en":[{"name":"Enomoto A"},{"name":"Suzuki N"},{"name":"Hirano K"},{"name":"Matsumoto Y"},{"name":"Morita Akinori"},{"name":"Sakai K"},{"name":"Koyama H"}],"ja":[{"name":"Enomoto A"},{"name":"Suzuki N"},{"name":"Hirano K"},{"name":"Matsumoto Y"},{"name":"森田 明典"},{"name":"Sakai K"},{"name":"Koyama H"}]},"description":{"en":"We found that SAPK/JNK was phosphorylated during X-ray-induced rapid cell death of MOLT-4 cells and that acid Sphingomyelinase inhibitor D609 suppressed the rapid cell death as well as phosphorylation of SAPK/JNK. Also C2-ceramide caused phosphorylation of SAPK/JNK, followed by rapid cell death. Further we isolated X-ray-resistant radiation-hybrid clones from MOLT-4 and 50 Gy irradiated mouse FM3A cells by repeated selections with 3 Gy irradiation. One of them named Rh-1a was found resistant to X-ray- as well as C2-ceramide-induced rapid cell death. Rh-1a cells had mouse DNA but no increase in either mouse or human Bcl-2 determined by Western blotting. Accumulation of p53 after X-irradiation was similarly observed in both parental MOLT-4 and Rh-1a cells. However, contrasting to prolonged and prominent phosphorylated status of SAPK/JNK in MOLT-4 cells, Rh-1a cells exhibited short transient increase and FM3A cells showed no increase of phosphorylated status SAPK/JNK after X-irradiation. Therefore, SAPK/JNK activation is considered important in X-ray-induced rapid cell death or apoptosis of MOLT-4 cells.","ja":"We found that SAPK/JNK was phosphorylated during X-ray-induced rapid cell death of MOLT-4 cells and that acid Sphingomyelinase inhibitor D609 suppressed the rapid cell death as well as phosphorylation of SAPK/JNK. Also C2-ceramide caused phosphorylation of SAPK/JNK, followed by rapid cell death. Further we isolated X-ray-resistant radiation-hybrid clones from MOLT-4 and 50 Gy irradiated mouse FM3A cells by repeated selections with 3 Gy irradiation. One of them named Rh-1a was found resistant to X-ray- as well as C2-ceramide-induced rapid cell death. Rh-1a cells had mouse DNA but no increase in either mouse or human Bcl-2 determined by Western blotting. Accumulation of p53 after X-irradiation was similarly observed in both parental MOLT-4 and Rh-1a cells. However, contrasting to prolonged and prominent phosphorylated status of SAPK/JNK in MOLT-4 cells, Rh-1a cells exhibited short transient increase and FM3A cells showed no increase of phosphorylated status SAPK/JNK after X-irradiation. Therefore, SAPK/JNK activation is considered important in X-ray-induced rapid cell death or apoptosis of MOLT-4 cells."},"publication_date":"2000-07","publication_name":{"en":"Cancer Letters","ja":"Cancer Letters"},"volume":"Vol.155","number":"No.2","starting_page":"137","ending_page":"144","languages":["eng"],"referee":true,"identifiers":{"issn":["0304-3835"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:46, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10922471","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265100","label":"url"}],"paper_title":{"en":"Cleavage and phosphorylation of XRCC4 protein induced by X-irradiation.","ja":"Cleavage and phosphorylation of XRCC4 protein induced by X-irradiation."},"authors":{"en":[{"name":"Matsumoto Y"},{"name":"Suzuki N"},{"name":"Namba N"},{"name":"Umeda N"},{"name":"Ma X J"},{"name":"Morita Akinori"},{"name":"Tomita M"},{"name":"Enomoto A"},{"name":"Serizawa S"},{"name":"Hirano K"},{"name":"Sakaia K"},{"name":"Yasuda H"},{"name":"Hosoi Y"}],"ja":[{"name":"Matsumoto Y"},{"name":"Suzuki N"},{"name":"Namba N"},{"name":"Umeda N"},{"name":"Ma X J"},{"name":"森田 明典"},{"name":"Tomita M"},{"name":"Enomoto A"},{"name":"Serizawa S"},{"name":"Hirano K"},{"name":"Sakaia K"},{"name":"Yasuda H"},{"name":"Hosoi Y"}]},"description":{"en":"We report the p35 and p60 forms of XRCC4 protein, appearing in human leukemia MOLT-4 or U937 cells following X-irradiation or hyperthermia. p35 appeared in conjunction with the cleavage of DNA-dependent protein kinase catalytic subunit (DNA-PKcs) and the fragmentation of internucleosomal DNA, and was suppressed by Ac-DEVD-CHO. p35 was also produced in vitro by treating MOLT-4 cell lysate with recombinant caspases, suggesting that p35 was a caspase-cleaved fragment of XRCC4 in apoptotic cell death. p60 was sensitive to treatment with phosphatase or wortmannin and was undetectable in M059J cells deficient in DNA-PKcs. However, p60 was found in ataxia-telangiectasia cells after irradiation. These results indicated p60 as a phosphorylated form of XRCC4, requiring DNA-PKcs but not ataxia-telangiectasia mutated (ATM).","ja":"We report the p35 and p60 forms of XRCC4 protein, appearing in human leukemia MOLT-4 or U937 cells following X-irradiation or hyperthermia. p35 appeared in conjunction with the cleavage of DNA-dependent protein kinase catalytic subunit (DNA-PKcs) and the fragmentation of internucleosomal DNA, and was suppressed by Ac-DEVD-CHO. p35 was also produced in vitro by treating MOLT-4 cell lysate with recombinant caspases, suggesting that p35 was a caspase-cleaved fragment of XRCC4 in apoptotic cell death. p60 was sensitive to treatment with phosphatase or wortmannin and was undetectable in M059J cells deficient in DNA-PKcs. However, p60 was found in ataxia-telangiectasia cells after irradiation. These results indicated p60 as a phosphorylated form of XRCC4, requiring DNA-PKcs but not ataxia-telangiectasia mutated (ATM)."},"publication_date":"2000-07-28","publication_name":{"en":"FEBS Letters","ja":"FEBS Letters"},"volume":"Vol.478","number":"No.1-2","starting_page":"67","ending_page":"71","languages":["eng"],"referee":true,"identifiers":{"issn":["0014-5793"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:47, {"insert":{"user_id":"6000005112","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/10760692","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=265097","label":"url"}],"paper_title":{"en":"Increased expression after X-irradiation of MUC1 in cultured human colon carcinoma HT-29 cells.","ja":"Increased expression after X-irradiation of MUC1 in cultured human colon carcinoma HT-29 cells."},"authors":{"en":[{"name":"Kang Y"},{"name":"Hirano K"},{"name":"Suzuki N"},{"name":"Enomoto A"},{"name":"Morita Akinori"},{"name":"Irimura T"},{"name":"Sakai K"}],"ja":[{"name":"Kang Y"},{"name":"Hirano K"},{"name":"Suzuki N"},{"name":"Enomoto A"},{"name":"森田 明典"},{"name":"Irimura T"},{"name":"Sakai K"}]},"description":{"en":"The effect of X-irradiation on production of MUC1 was studied with human colon carcinoma HT-29 cells. As evaluated by immunocytochemical staining, the percentages of MUC1-positive cells in cells at 4 days after 6 Gy irradiation and in unirradiated control cells were 52 +/- 3.5% (n = 6) and 26 +/- 2.8% (n = 6), respectively. Flow-cytometric analysis of living cells showed that MUC1 began to rise from day 1, reaching a plateau by day 4 after 6 Gy irradiation. Western blot analysis with monoclonal antibody MY.1E12 against glycosylated MUC1 (mature form) showed dose-dependent increases of two bands (500 and 390 kDa) corresponding to two polymorphic MUC1 alleles. Premature forms of MUC1 (350 and 240 kDa) were detectable with monoclonal antibody HMFG-2 only in irradiated cells, suggesting that new core protein synthesis had been induced. The transcriptional activity of the MUC1 gene was analyzed in terms of transient expression of MUC1-CAT reporter plasmids containing 5'-flanking sequences of the MUC1 gene fused to the bacterial chloramphenicol acetyltransferase (CAT) gene. The results of CAT assay indicate that enhanced expression of MUC1 in irradiated HT-29 cells was due to upregulation of MUC1 transcription, and required the upstream promoter.","ja":"The effect of X-irradiation on production of MUC1 was studied with human colon carcinoma HT-29 cells. As evaluated by immunocytochemical staining, the percentages of MUC1-positive cells in cells at 4 days after 6 Gy irradiation and in unirradiated control cells were 52 +/- 3.5% (n = 6) and 26 +/- 2.8% (n = 6), respectively. Flow-cytometric analysis of living cells showed that MUC1 began to rise from day 1, reaching a plateau by day 4 after 6 Gy irradiation. Western blot analysis with monoclonal antibody MY.1E12 against glycosylated MUC1 (mature form) showed dose-dependent increases of two bands (500 and 390 kDa) corresponding to two polymorphic MUC1 alleles. Premature forms of MUC1 (350 and 240 kDa) were detectable with monoclonal antibody HMFG-2 only in irradiated cells, suggesting that new core protein synthesis had been induced. The transcriptional activity of the MUC1 gene was analyzed in terms of transient expression of MUC1-CAT reporter plasmids containing 5'-flanking sequences of the MUC1 gene fused to the bacterial chloramphenicol acetyltransferase (CAT) gene. The results of CAT assay indicate that enhanced expression of MUC1 in irradiated HT-29 cells was due to upregulation of MUC1 transcription, and required the upstream promoter."},"publication_date":"2000-03","publication_name":{"en":"Gann : Japanese Journal of Cancer Research","ja":"Gann : Japanese Journal of Cancer Research"},"volume":"Vol.91","number":"No.3","starting_page":"324","ending_page":"330","languages":["eng"],"referee":true,"identifiers":{"issn":["0910-5050"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
==== end registerFile(/WWW/pub2/data/ERD/person/264516/researchmap/published_papers.jsonl, wD7LNpMBwbWENEENQiXO) ====
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line:1, {"insert":{"user_id":"6000005112","type":"misc","id":"46003219"},"force":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1390580936920512640/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=406041","label":"url"}],"paper_title":{"en":"Molecular Mechanisms of Acute Radiation Intestinal Injury and Its Control","ja":"Molecular Mechanisms of Acute Radiation Intestinal Injury and Its Control"},"authors":{"en":[{"name":"Morita Akinori"},{"name":"Nishiyama Yuichi"},{"name":"Sakai Takuma"},{"name":"Higashi Yuichi"}],"ja":[{"name":"森田 明典"},{"name":"西山 祐一"},{"name":"坂井 卓磨"},{"name":"東 優一"}]},"publication_date":"2024-02-28","publication_name":{"en":"Radiation Environment and Medicine","ja":"Radiation Environment and Medicine"},"volume":"Vol.13","number":"No.1","starting_page":"10","ending_page":"18","languages":["eng"],"invited":true,"identifiers":{"doi":["10.51083/radiatenvironmed.13.1_10"],"issn":["2423-9097"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
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