=== 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/201602/researchmap/published_papers-propagate.jsonl) ====
line:1, {"insert":{"user_id":"R000010784","type":"published_papers"},"similar_merge":{"see_also":[{"@id":"https://tokushima-u.repo.nii.ac.jp/records/2012197","label":"url"},{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/39032464","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=409647","label":"url"}],"paper_title":{"en":"Pro-cathepsin D prevents aberrant protein aggregation dependent on endoplasmic reticulum protein CLN6.","ja":"Pro-cathepsin D prevents aberrant protein aggregation dependent on endoplasmic reticulum protein CLN6."},"authors":{"en":[{"name":"Shiro Yuki"},{"name":"Katayama Syouichi"},{"name":"Tsukamoto Haruka"},{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"城 裕己"},{"name":"片山 将一"},{"name":"塚本 陽花"},{"name":"山﨑 哲男"}]},"description":{"en":"We previously expressed a chimeric protein in which the small heat-shock protein αB-crystallin (αBC) is fused at its N-terminus to the C-terminus of the first transmembrane segment of the endoplasmic reticulum (ER) protein mitsugumin 23 and confirmed its localization to the ER. Moreover, overexpression of this N-terminally modified αBC was shown to prevent the aggregation of the coexpressed R120G αBC variant, which is highly aggregation-prone and associated with the hereditary myopathy αB-crystallinopathy. To uncover a molecular mechanism by which the ER-anchored αBC negatively regulates the protein aggregation, we isolated proteins that bind to the ER-anchored αBC and identified the lysosomal protease cathepsin D (CTSD) as one such interacting protein. Proteolytically active CTSD is produced by multi-step processing of pro-cathepsin D (proCTSD), which is initially synthesized in the ER and delivered to lysosomes. When overexpressed, CTSD itself prevented the coexpressed R120G αBC variant from aggregating. This anti-aggregate activity was also elicited upon overexpression of the W383C CTSD variant, which is predominantly sequestered in the ER and consequently remains unprocessed, suggesting that proCTSD, rather than mature CTSD, serves to suppress the aggregation of the R120G αBC variant. Meanwhile, overexpression of the A58V CTSD variant, which is identical to wild-type CTSD except for the Ala58Val substitution within the pro-peptide, did not suppress the protein aggregation, indicating that the integrity of the pro-peptide is required for proCTSD to exert its anti-aggregate activity. Based on our previous finding that overexpression of the ER transmembrane protein CLN6 (ceroid-lipofuscinosis, neuronal 6), identified as an interacting protein of the ER-anchored αBC, prevents the R120G αBC variant from aggregating, the CLN6-proCTSD coupling was hypothesized to underpin the functionality of proCTSD within the ER. Indeed, CTSD, when overexpressed in CLN6-depleted cells, was unable to exert its anti-aggregate activity, supporting our view. Collectively, we show here that proCTSD prevents the protein aggregation through the functional association with CLN6 in the microenvironment surrounding the ER membrane, shedding light on a novel aspect of proCTSD and its potential involvement in CTSD-related disorders characterized by the accumulation of aberrant protein aggregates.","ja":"We previously expressed a chimeric protein in which the small heat-shock protein αB-crystallin (αBC) is fused at its N-terminus to the C-terminus of the first transmembrane segment of the endoplasmic reticulum (ER) protein mitsugumin 23 and confirmed its localization to the ER. Moreover, overexpression of this N-terminally modified αBC was shown to prevent the aggregation of the coexpressed R120G αBC variant, which is highly aggregation-prone and associated with the hereditary myopathy αB-crystallinopathy. To uncover a molecular mechanism by which the ER-anchored αBC negatively regulates the protein aggregation, we isolated proteins that bind to the ER-anchored αBC and identified the lysosomal protease cathepsin D (CTSD) as one such interacting protein. Proteolytically active CTSD is produced by multi-step processing of pro-cathepsin D (proCTSD), which is initially synthesized in the ER and delivered to lysosomes. When overexpressed, CTSD itself prevented the coexpressed R120G αBC variant from aggregating. This anti-aggregate activity was also elicited upon overexpression of the W383C CTSD variant, which is predominantly sequestered in the ER and consequently remains unprocessed, suggesting that proCTSD, rather than mature CTSD, serves to suppress the aggregation of the R120G αBC variant. Meanwhile, overexpression of the A58V CTSD variant, which is identical to wild-type CTSD except for the Ala58Val substitution within the pro-peptide, did not suppress the protein aggregation, indicating that the integrity of the pro-peptide is required for proCTSD to exert its anti-aggregate activity. Based on our previous finding that overexpression of the ER transmembrane protein CLN6 (ceroid-lipofuscinosis, neuronal 6), identified as an interacting protein of the ER-anchored αBC, prevents the R120G αBC variant from aggregating, the CLN6-proCTSD coupling was hypothesized to underpin the functionality of proCTSD within the ER. Indeed, CTSD, when overexpressed in CLN6-depleted cells, was unable to exert its anti-aggregate activity, supporting our view. Collectively, we show here that proCTSD prevents the protein aggregation through the functional association with CLN6 in the microenvironment surrounding the ER membrane, shedding light on a novel aspect of proCTSD and its potential involvement in CTSD-related disorders characterized by the accumulation of aberrant protein aggregates."},"publication_date":"2024-07-16","publication_name":{"en":"Molecular Genetics and Metabolism","ja":"Molecular Genetics and Metabolism"},"volume":"143","number":"1-2","starting_page":"108539","ending_page":"108539","languages":["eng"],"referee":true,"identifiers":{"doi":["10.1016/j.ymgme.2024.108539"],"issn":["1096-7206"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:2, {"insert":{"user_id":"R000010784","type":"published_papers","id":"30377063"},"force":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/21685326","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=233810","label":"url"}],"paper_title":{"en":"A Requirement for the p85 PI3K Adapter Protein BCAP in the Protection of Macrophages from Apoptosis Induced by Endoplasmic Reticulum Stress.","ja":"A Requirement for the p85 PI3K Adapter Protein BCAP in the Protection of Macrophages from Apoptosis Induced by Endoplasmic Reticulum Stress."},"authors":{"en":[{"name":"Song Sungwon"},{"name":"Chew Claude"},{"name":"Dale M. Benjamin"},{"name":"Traum Daniel"},{"name":"Peacock James"},{"name":"Yamazaki Tetsuo"},{"name":"Clynes Raphael"},{"name":"Kurosaki Tomohiro"},{"name":"Greenberg Steven"}],"ja":[{"name":"Song Sungwon"},{"name":"Chew Claude"},{"name":"Dale M. Benjamin"},{"name":"Traum Daniel"},{"name":"Peacock James"},{"name":"山﨑 哲男"},{"name":"Clynes Raphael"},{"name":"Kurosaki Tomohiro"},{"name":"Greenberg Steven"}]},"description":{"en":"Macrophages are innate immune cells that play key roles in regulation of the immune response and in tissue injury and repair. In response to specific innate immune stimuli, macrophages may exhibit signs of endoplasmic reticulum (ER) stress and progress to apoptosis. Factors that regulate macrophage survival under these conditions are poorly understood. In this study, we identified B cell adapter protein (BCAP), a p85 PI3K-binding adapter protein, in promoting survival in response to the combined challenge of LPS and ER stress. BCAP was unique among nine PI3K adapter proteins in being induced >10-fold in response to LPS. LPS-stimulated macrophages incubated with thapsigargin, a sarcoplasmic/endoplasmic reticulum calcium ATPase inhibitor that induces ER stress, underwent caspase-3 activation and apoptosis. Macrophages from BCAP(-/-) mice exhibited increased apoptosis in response to these stimuli. BCAP-deficient macrophages demonstrated decreased activation of Akt, but not ERK, and, unlike BCAP-deficient B cells, expressed normal amounts of the NF-B subunits, c-Rel and RelA. Retroviral transduction of BCAP-deficient macrophages with wild-type BCAP, but not a Y4F BCAP mutant defective in binding the SH2 domain of p85 PI3K, reversed the proapoptotic phenotype observed in BCAP-deficient macrophages. We conclude that BCAP is a nonredundant PI3K adapter protein in macrophages that is required for maximal cell survival in response to ER stress. We suggest that as macrophages engage their pathogenic targets, innate immune receptors trigger increased expression of BCAP, which endows them with the capacity to withstand further challenges from ongoing cellular insults, such as ER stress.","ja":"Macrophages are innate immune cells that play key roles in regulation of the immune response and in tissue injury and repair. In response to specific innate immune stimuli, macrophages may exhibit signs of endoplasmic reticulum (ER) stress and progress to apoptosis. Factors that regulate macrophage survival under these conditions are poorly understood. In this study, we identified B cell adapter protein (BCAP), a p85 PI3K-binding adapter protein, in promoting survival in response to the combined challenge of LPS and ER stress. BCAP was unique among nine PI3K adapter proteins in being induced >10-fold in response to LPS. LPS-stimulated macrophages incubated with thapsigargin, a sarcoplasmic/endoplasmic reticulum calcium ATPase inhibitor that induces ER stress, underwent caspase-3 activation and apoptosis. Macrophages from BCAP(-/-) mice exhibited increased apoptosis in response to these stimuli. BCAP-deficient macrophages demonstrated decreased activation of Akt, but not ERK, and, unlike BCAP-deficient B cells, expressed normal amounts of the NF-B subunits, c-Rel and RelA. Retroviral transduction of BCAP-deficient macrophages with wild-type BCAP, but not a Y4F BCAP mutant defective in binding the SH2 domain of p85 PI3K, reversed the proapoptotic phenotype observed in BCAP-deficient macrophages. We conclude that BCAP is a nonredundant PI3K adapter protein in macrophages that is required for maximal cell survival in response to ER stress. We suggest that as macrophages engage their pathogenic targets, innate immune receptors trigger increased expression of BCAP, which endows them with the capacity to withstand further challenges from ongoing cellular insults, such as ER stress."},"publication_date":"2011-06-17","publication_name":{"en":"The Journal of Immunology","ja":"The Journal of Immunology"},"volume":"187","number":"2","starting_page":"619","ending_page":"625","languages":["eng"],"referee":true,"identifiers":{"doi":["10.4049/jimmunol.0903425"],"issn":["1550-6606"]},"published_paper_type":"scientific_journal"},"priority":"input_data"}
line:3, {"insert":{"user_id":"R000010784","type":"published_papers","id":"47280208"},"force":{"see_also":[{"@id":"https://www.sciencedirect.com/science/article/pii/S109671922101115X?via%3Dihub","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=410652","label":"url"}],"paper_title":{"en":"Novel insight into the compound heterozygosity-driven CLN6 disease pathomechanism","ja":"Novel insight into the compound heterozygosity-driven CLN6 disease pathomechanism"},"authors":{"en":[{"name":"Shiro Yuki"},{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"城 裕己"},{"name":"山﨑 哲男"}]},"publication_date":"2022-02","publication_name":{"en":"Molecular Genetics and Metabolism","ja":"Molecular Genetics and Metabolism"},"volume":"135","number":"2","starting_page":"S112","ending_page":"S112","languages":["eng"],"identifiers":{"doi":["10.1016/j.ymgme.2021.11.297"],"issn":["1096-7206"]},"published_paper_type":"research_institution"},"priority":"input_data"}
==== end registerFile(/WWW/pub2/data/ERD/person/201602/researchmap/published_papers-propagate.jsonl, wFNiiKABn_HdSsNV6nWv) ====
==== begin registerFile(/WWW/pub2/data/ERD/person/201602/researchmap/misc-propagate.jsonl) ====
line:1, {"insert":{"user_id":"R000010784","type":"misc","id":"36260686"},"force":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1520294429647353216/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=384000","label":"url"}],"paper_title":{"en":"運動療法とロボティクスの動向―近未来予測―. 筋ジストロフィーの診療・リハビリテーション医療の動向","ja":"運動療法とロボティクスの動向―近未来予測―. 筋ジストロフィーの診療・リハビリテーション医療の動向"},"authors":{"en":[{"name":"Takata Shinjiro"},{"name":"森脇 好乃美"},{"name":"森脇 笙"},{"name":"馬渕 勝"},{"name":"岩田 織江"},{"name":"国重 裕二"},{"name":"澤田 侑樹"},{"name":"吉兼 麻木子"},{"name":"宮崎 達志"},{"name":"近藤 梨恵子"},{"name":"渡邊 典子"},{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"髙田 信二郎"},{"name":"森脇 好乃美"},{"name":"森脇 笙"},{"name":"馬渕 勝"},{"name":"岩田 織江"},{"name":"国重 裕二"},{"name":"澤田 侑樹"},{"name":"吉兼 麻木子"},{"name":"宮崎 達志"},{"name":"近藤 梨恵子"},{"name":"渡邊 典子"},{"name":"山﨑 哲男"}]},"publication_date":"2022-01-27","publication_name":{"en":"Journal of Clinical Rehabilitation","ja":"Journal of Clinical Rehabilitation"},"volume":"31","number":"2","starting_page":"134","ending_page":"142","languages":["jpn"],"identifiers":{"issn":["0918-5259"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:2, {"insert":{"user_id":"R000010784","type":"misc","id":"33312369"},"force":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1523951030943292672/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=378585","label":"url"}],"paper_title":{"en":"大腿骨近位部骨折回避のための転倒予防の重要性と具体策 : サルコペニアとフレイルからのアプローチを含む (第47回 日本股関節学会学術集会 シンポジウム2 大腿骨近位部骨折の予防と治療における新たな知見と進歩を目指して)","ja":"大腿骨近位部骨折回避のための転倒予防の重要性と具体策 : サルコペニアとフレイルからのアプローチを含む (第47回 日本股関節学会学術集会 シンポジウム2 大腿骨近位部骨折の予防と治療における新たな知見と進歩を目指して)"},"authors":{"en":[{"name":"Takata Shinjiro"},{"name":"森脇 笙"},{"name":"Ueda Yuka"},{"name":"元木 由美"},{"name":"森脇 好乃美"},{"name":"Yamazaki Tetsuo"},{"name":"田村 英司"},{"name":"住友 祐介"},{"name":"柿本 直子"},{"name":"海部 忍"}],"ja":[{"name":"髙田 信二郎"},{"name":"森脇 笙"},{"name":"上田 由佳"},{"name":"元木 由美"},{"name":"森脇 好乃美"},{"name":"山﨑 哲男"},{"name":"田村 英司"},{"name":"住友 祐介"},{"name":"柿本 直子"},{"name":"海部 忍"}]},"publication_date":"2021-02","publication_name":{"en":"The Journal of Japan Osteoporosis Society","ja":"日本骨粗鬆症学会雑誌"},"volume":"7","number":"2","starting_page":"358","ending_page":"363","languages":["jpn"],"identifiers":{"issn":["2189-8383"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:3, {"insert":{"user_id":"R000010784","type":"misc"},"similar_merge":{"see_also":[{"@id":"https://www.ncbi.nlm.nih.gov/pubmed/18064887","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=215075","label":"url"}],"paper_title":{"en":"[Molecular basis of ryanodine receptor-mediated Ca2+ release]","ja":"[Molecular basis of ryanodine receptor-mediated Ca2+ release]"},"authors":{"en":[{"name":"Ikeda Atsushi"},{"name":"Yamazaki Tetsuo"},{"name":"Takeshima Hiroshi"}],"ja":[{"name":"Ikeda Atsushi"},{"name":"山﨑 哲男"},{"name":"Takeshima Hiroshi"}]},"publication_date":"2007-12","publication_name":{"en":"Tanpakushitsu Kakusan Koso","ja":"蛋白質・核酸・酵素"},"volume":"52","number":"15","starting_page":"1965","ending_page":"1972","languages":["jpn"],"identifiers":{"issn":["0039-9450"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:4, {"insert":{"user_id":"R000010784","type":"misc"},"similar_merge":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/40006740714/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=234635","label":"url"}],"paper_title":{"en":"B細胞の分化・機能発現とBCAP","ja":"B細胞の分化・機能発現とBCAP"},"authors":{"en":[{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"山﨑 哲男"}]},"publication_date":"2005-04","publication_name":{"en":"Clinical Immunology","ja":"臨床免疫"},"volume":"43","number":"4","starting_page":"483","ending_page":"486","languages":["jpn"],"identifiers":{"issn":["0386-9695"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:5, {"insert":{"user_id":"R000010784","type":"misc"},"similar_merge":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/40006532147/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=234634","label":"url"}],"paper_title":{"en":"B細胞の最終分化を決定するBCAPの核内転写因子c-Rel制御 (免疫細胞のシグナル伝達)","ja":"B細胞の最終分化を決定するBCAPの核内転写因子c-Rel制御 (免疫細胞のシグナル伝達)"},"authors":{"en":[{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"山﨑 哲男"}]},"publication_date":"2005","publication_name":{"en":"免疫","ja":"免疫"},"volume":"2005","starting_page":"165","ending_page":"170","languages":["jpn"],"identifiers":{"issn":["0918-6557"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:6, {"insert":{"user_id":"R000010784","type":"misc","id":"30377091"},"force":{"see_also":[{"@id":"https://cir.nii.ac.jp/crid/1520573330734682624/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=378582","label":"url"}],"paper_title":{"en":"成熟B細胞の維持におけるB cell adaptor for PI3 kinase(BCAP)の役割","ja":"成熟B細胞の維持におけるB cell adaptor for PI3 kinase(BCAP)の役割"},"authors":{"en":[{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"山﨑 哲男"}]},"publication_date":"2004-05","publication_name":{"en":"Clinical Immunology","ja":"臨床免疫"},"volume":"41","number":"5","starting_page":"574","ending_page":"577","languages":["jpn"],"identifiers":{"issn":["0386-9695"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:7, {"insert":{"user_id":"R000010784","type":"misc"},"similar_merge":{"see_also":[{"@id":"http://ci.nii.ac.jp/naid/40006253664/","label":"url"},{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=234633","label":"url"}],"paper_title":{"en":"成熟B細胞の維持におけるB cell adaptor for PI3 kinase(BCAP)の役割","ja":"成熟B細胞の維持におけるB cell adaptor for PI3 kinase(BCAP)の役割"},"authors":{"en":[{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"山﨑 哲男"}]},"publication_date":"2004-05","publication_name":{"en":"Clinical Immunology","ja":"臨床免疫"},"volume":"41","number":"5","starting_page":"574","ending_page":"577","languages":["jpn"],"identifiers":{"issn":["0386-9695"]},"misc_type":"introduction_scientific_journal"},"priority":"input_data"}
line:8, {"insert":{"user_id":"R000010784","type":"misc","id":"41876157"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=394932","label":"url"}],"paper_title":{"en":"令和4年度 徳島大学高等教育研究センターアドミッション部門 報告書","ja":"令和4年度 徳島大学高等教育研究センターアドミッション部門 報告書"},"authors":{"en":[{"name":"Ueno Yoshihiko"},{"name":"Seki Yosuke"},{"name":"Kinugawa Satoshi"},{"name":"Morioka Hisayoshi"},{"name":"Takahashi Akira"},{"name":"Mori Kenji"},{"name":"Ishimaru Naozumi"},{"name":"Ozaki Kazumi"},{"name":"Yamazaki Tetsuo"},{"name":"Takada Atsushi"},{"name":"Uto Yoshihiro"},{"name":"Saito Takahito"},{"name":"Kamioka Maiko"}],"ja":[{"name":"植野 美彦"},{"name":"関 陽介"},{"name":"衣川 仁"},{"name":"森岡 久尚"},{"name":"髙橋 章"},{"name":"森 健治"},{"name":"石丸 直澄"},{"name":"尾崎 和美"},{"name":"山﨑 哲男"},{"name":"高田 篤"},{"name":"宇都 義浩"},{"name":"齊藤 隆仁"},{"name":"上岡 麻衣子"}]},"publication_date":"2023-03","publication_name":{"en":"令和4年度 徳島大学高等教育研究センターアドミッション部門 報告書","ja":"令和4年度 徳島大学高等教育研究センターアドミッション部門 報告書"},"languages":["jpn"],"misc_type":"others"},"priority":"input_data"}
==== end registerFile(/WWW/pub2/data/ERD/person/201602/researchmap/misc-propagate.jsonl, DFNjiKABn_HdSsNVOXZo) ====
==== begin registerFile(/WWW/pub2/data/ERD/person/201602/researchmap/presentations-propagate.jsonl) ====
line:1, {"insert":{"user_id":"R000010784","type":"presentations","id":"42454133"},"force":{"see_also":[{"@id":"https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?EID=397803","label":"url"}],"presentation_title":{"en":"Cathepsin Dは小胞体内腔でCLN6の凝集抑制能を支える","ja":"Cathepsin Dは小胞体内腔でCLN6の凝集抑制能を支える"},"presenters":{"en":[{"name":"Shiro Yuki"},{"name":"Yamazaki Tetsuo"}],"ja":[{"name":"城 裕己"},{"name":"山﨑 哲男"}]},"event":{"en":"第21回四国免疫フォーラム","ja":"第21回四国免疫フォーラム"},"publication_date":"2023-06-03","languages":["jpn"],"location":{"en":"徳島市","ja":"徳島市"},"is_international_presentation":false},"priority":"input_data"}
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