Hsp47とは？ わかりやすく解説

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Hsp47

(Heat-Shock Protein 47 から転送)

出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2024/03/06 06:17 UTC 版)

Hsp47（熱ショックタンパク質 (Heat shock protein) 47）は、コラーゲンに関し、人間のタンパク質シャペロンの１つとして機能するセルピンである[5][6]。SERPINH1 としても知られる。熱ショックタンパク質としては、1986年に初めて報告された[7]。


参考文献
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000149257 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000070436 - Ensembl, May 2017
  3. ^ Human PubMed Reference:
  4. ^ Mouse PubMed Reference:
  5. ^ a b “Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)”. 2021年12月19日閲覧。
  6. ^ Dafforn TR; Della M; Miller AD (2001-12). “The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis”. The Journal of Biological Chemistry 276 (52): 49310–9. doi:10.1074/jbc.M108896200. PMID 11592970. 
  7. ^ a b c K. Nagata; S. Saga; K. M. Yamada (1986). “A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein”. Journal of Cell Biology 103 (1): 223–229. doi:10.1083/jcb.103.1.223. PMC 2113802. PMID 3722264. https://doi.org/10.1083/jcb.103.1.223. 
  8. ^ a b Christy A. Thomson; Vettai S. Ananthanarayanan (2000-8-1). “Structure-function studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro”. Biochemcal Journal (3): 877–83. doi:10.1042/bj3490877. PMC 1221217. PMID 10903151. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221217/. 
  9. ^ a b Ito S; Nagata K. (2019-2-8). Jornal of Biological Chemistry 294 (6): 2133–41. doi:10.1074/jbc.TM118.002812. PMC 6369284. PMID 30541925. https://www.jbc.org/article/S0021-9258(20)36857-5/fulltext. 
  10. ^ Denisse Sepulveda; Diego Rojas-Rivera, Diego A Rodríguez, Jody Groenendyk, Andres Köhler, Cynthia Lebeaupin, Shinya Ito, Hery Urra, Amado Carreras-Sureda, Younis Hazari, Mireille Vasseur-Cognet, Maruf M U Ali, Eric Chevet, Gisela Campos, Patricio Godoy, Tomas Vaisar, Béatrice Bailly-Maitre, Kazuhiro Nagata, Marek Michalak, Jimena Sierralta, Claudio Hetz (2018-1-18). “Interactome screening identifies the ER luminal chaperone Hsp47 as a regulator of the unfolded protein response transducer IRE1α”. Molecular Cell 69 (2): 238–252.e237. doi:10.1016/j.molcel.2017.12.028. PMID 29351844. https://www.cell.com/molecular-cell/fulltext/S1097-2765(17)31007-9. 
  11. ^ Akihiro Yoneda; Kaori Sakai-Sawada; Kenjiro Minomi; Yasuaki Tamura (2020-6). “Heat shock protein 47 maintains cancer cell growth by inhibiting the unfolded protein response transducer IRE1a”. Molecular Cancer Research (6): 847–58. doi:10.1158/1541-7786.MCR-19-0673. PMID 32102897. https://mcr.aacrjournals.org/content/18/6/847.long. 
  12. ^ Williams, R. Sanders (2000-3-21). “Heat Shock Protein 47: A Chaperone for the Fibrous Cap?” (英語). Circulation 101 (11): 1227–1228. doi:10.1161/01.CIR.101.11.1227. PMID 10725278. http://circ.ahajournals.org/content/101/11/1227.full 2017年12月11日閲覧。. 
  13. ^ a b Mohammed, Tasab; Margaret R., Batten; Neil J., Bulleid (2000-5-15). “Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen.”. EMBO Journal (10): 2204–11. doi:10.1093/emboj/19.10.2204. PMC 384358. PMID 10811611. https://doi.org/10.1093/emboj/19.10.2204. 
  14. ^ Takashi Ono; Takahiro Miyazaki; Yoshihito Ishida; Masayoshi Uehata; Kazuhiro Nagata (2012-2). “Direct in Vitro and in Vivo Evidence for Interaction between Hsp47 Protein and Collagen Triple Helix”. Glycobiology and Extracellular Matrices 287 (9): 6810–18. doi:10.1074/jbc.M111.280248. PMC 3307285. PMID 22235129. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3307285/. 
  15. ^ a b Naoko Nagai; Masanori Hosokawa; Shigeyoshi Itohara; Eijiro Adachi; Takatoshi Matsushita; Nobuko Hosokawa; Kazuhiro Nagata (2000). “Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis”. Journal of Cell Biology 150 (6): 1499–1506. doi:10.1083/jcb.150.6.1499. PMC 2150697. PMID 10995453. https://rupress.org/jcb/article/150/6/1499/45517/Embryonic-Lethality-of-Molecular-Chaperone-Hsp47. 
  16. ^ Yoshihito Ishida; Hiroshi Kubota; Akitsugu Yamamoto; Akira Kitamura; Hans Peter Bächinger; Kazuhiro Nagata (2006-5). “Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis”. Molecular Biology of the Cell 17 (5): 2346–55. doi:10.1091/mbc.E05-11-1065. PMC 1446091. PMID 16525016. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1446091/. 
  17. ^ イヌにつき、Cord Drögemüller; Doreen Becker, Adrian Brunner, Bianca Haase, Patrick Kircher, Frank Seeliger, Michael Fehr, Ulrich Baumann, Kerstin Lindblad-Toh, Tosso Leeb (2009-7-24). “A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta.”. PLoS Genetics 5. doi:10.1371/journal.pgen.1000579. PMC 2708911. PMID 19629171. https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1000579. 
  18. ^ ヒトにつき、Helena E. Christiansen; Ulrike Schwarze, Shawna M. Pyott, Abdulrahman AlSwaid, Mohammed Al Balwi, Shatha Alrasheed, Melanie G. Pepin, Mary Ann Weis, David R. Eyre, Peter H. Byers (2010-3-12). “Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta.”. American Journal of Human Genetics (3): 389–98. doi:10.1016/j.ajhg.2010.01.034. PMC 2833387. PMID 20188343. https://www.ncbi.nlm.nih.gov/sites/ppmc/articles/PMC2833387/. 
  19. ^ a b c Shingo Miyata; Tatsunori Mizuno; Yoshihisa Koyama; Taiichi Katayama; Masaya Tohyama (2013-7-29). “The Endoplasmic Reticulum-Resident Chaperone Heat Shock Protein 47 Protects the Golgi Apparatus from the Effects of O-Glycosylation Inhibition”. PLoS ONE 8. doi:10.1371/journal.pone.0069732. PMC 3726774. PMID 23922785. https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0069732. 
  20. ^ John Geraldine Sandana Mala; Chellan Rose (2010-11). “Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?”. Life Sciences 87 (19–22): 579–86. doi:10.1016/j.lfs.2010.09.024. PMID 20888348. 
  21. ^ a b Takaki Koide; Yoshifumi Takahara; Shinichi Asada; Kazuhiro Nagata (2002-2). “Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47”. The Journal of Biology Chemistry 277 (8): 6178–82. doi:10.1074/jbc.M106497200. https://www.jbc.org/article/S0021-9258(19)82392-X/fulltext. 
  22. ^ a b Takaki Koide, coauthors = Yoshimi Nishikawa, Shinichi Asada, Chisato M. Yamazaki, Yoshifumi Takahara, Daisuke L. Homma, Akira Otaka, Katsuki Ohtani, Nobutaka Wakamiya, Kazuhiro Nagata, Kouki Kitagawa (2006-4-21). “Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins.”. The Journal of Biology Chemistry 281 (16): 11177–85. doi:10.1074/jbc.M601369200. PMID 16484215. https://www.jbc.org/article/S0021-9258(19)56296-2/fulltext. 
  23. ^ Haiyan Cai; Parvathy Sasikumar; Gemma Little; Dominique Bihan; Samir W Hamaia; Aiwu Zhou; Jonathan M Gibbins; Richard W Farndale (2021-7-3). “Identification of HSP47 Binding Site on Native Collagen and Its Implications for the Development of HSP47 Inhibitors”. Biomolecules (7): 983–94?. doi:10.3390/biom11070983. PMC 8301893. PMID 34356607. https://www.mdpi.com/2218-273X/11/7/983/htm. 
  24. ^ a b c Christine Widmer; Jan M. Gebauer; Elena Brunstein; Sabrina Rosenbaum; Frank Zaucke; Cord Drögemüller; Tosso Leeb; Ulrich Baumann (2012-8-14). “Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition”. Proceedings of the National Academy of Sciences of the United States of America 109 (no. 33): 13243–47. doi:10.1073/pnas.1208072109. PMC 3421173. PMID 22847422. https://doi.org/10.1073/pnas.1208072109. 
  25. ^ a b Sinan Oecal; Eileen Socher; Matthias Uthoff; Corvin Ernst; Frank Zaucke; Heinrich Sticht; Ulrich Baumann; Jan M Gebauer (2016-6-10). “The pH-dependent client release from the collagen-specific chaperone HSP47 is triggered by a tandem histidine pair”. Journal of Biological Chemistry (4): 12612–26. doi:10.1074/jbc.M115.706069. PMC 4933464. PMID 27129216. https://www.sciencedirect.com/science/article/pii/S0021925820409068?via%3Dihub. 
  26. ^ Mohd Firdaus Abdul-Wahab; Takayuki Homma; Michael Wright; Dee Olerenshaw; Timothy R Dafforn; Kazuhiro Nagata; Andrew D Miller (2013-2-8). “The pH sensitivity of murine heat shock protein 47 (HSP47) binding to collagen is affected by mutations in the breach histidine cluster”. J. Biol. Chem. (6): 4452–61. doi:10.1074/jbc.M112.409029. PMC 3567694. PMID 23212911. https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)46401-4. 
  27. ^ Shinichi Asada; Takaki Koide; Hiroyuki Yasui; Kazuhiro Nagata (1999). “Effect of HSP47 on Prolyl 4-Hydroxylation of Collagen Model Peptides”. Cell Structure and Function (日本細胞生物学会) (4): 187–96. doi:10.1247/csf.24.187. https://doi.org/10.1247/csf.24.187. 
  28. ^ Davide Eletto; Avinash Maganty, Daniela Eletto, Devin Dersh, Catherine Makarewich, Chhanda Biswas, James C. Paton, Adrienne W. Paton, Shirin Doroudgar, Christopher C. Glembotski, Yair Argon (2012-10-15). “Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response”. Journal of Cell Science 125: 4865–75. doi:10.1242/jcs.108928. PMID 22854046. https://doi.org/10.1242/jcs.10892. 
  29. ^ Nobuko Hosokawa; Hajime Takechi; Shinichi Yokota; Kazunori Hirayoshi; Kazuhiro Nagata (1993-4-30). “Structure of the gene encoding the mouse 47-kDa heat-shock protein (HSP47)”. Gene 126 (2): 187–93. doi:10.1016/0378-1119(93)90366-b. PMID 8482533. 
  30. ^ Maho Yagi-Utsumi; Sumi Yoshikawa, Yoshiki Yamaguchi, Yohei Nishi, Eiji Kurimoto, Yoshihito Ishida, Takayuki Homma, Jun Hoseki, Yoshimi Nishikawa, Takaki Koide, Kazuhiro Nagata, Koichi Kato (2012). “NMR and mutational identification of the collagen-binding site of the chaperone Hsp47”. PLoS ONE 7 (9): e45930. doi:10.1371/journal.pone.0045930. PMC 3457968. PMID 23049894. https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0045930. の図 S1
  31. ^ “Molecular Weight - HSP47 | HSP47”. 2022年2月12日閲覧。
  32. ^ Kazunori Hirayoshi; Hitoshi Kudo; Hajime Takechi; Akira Nakai; Akihiro Iwamatsu; Kenneth M Yamada; Kazuhiro Nagata (1991-8-1). “HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts”. Molecular and Cellular Biology (8): 4038, 4039. doi:10.1128/mcb.11.8.4036-4044.1991. PMC 361208. PMID 2072906. https://doi.org/10.1128/mcb.11.8.4036-4044.1991. 
  33. ^ a b 永田和宏、平芳一法「熱ショック蛋白質の発現と機能」『日本ハイパーサミア誌』第3巻第2号、日本ハイパーサーミア学会、1987年、144, 145、doi:10.3191/thermalmedicine.3.135。 
  34. ^ Cong-Xiao Gao; Eiji Miyoshi, Naofumi Uozumi, Rina Takamiya, Xiangchun Wang, Katsuhisa Noda, Jianguo Gu, Koichi Honke, Yoshinao Wada, Naoyuki Taniguchi (2005-11). “Bisecting GlcNAc mediates the binding of annexin V to Hsp47”. Glycobiology 15 (11): 1067–75. doi:10.1093/glycob/cwj005. PMID 16000695. https://academic.oup.com/glycob/article/15/11/1067/578291?login=false. 
  35. ^ Ming Chung Lin; Chung Hsi Hsing; Fu An Li; Chien Hsing Wu; Yaw Syan Fu; Jen Kun Cheng; Bin Huang (2014-1). “Rosuvastatin modulates the post-translational acetylome in endothelial cells”. Acta Cardiologica Sinica (1): 67–73. PMC 4804823. PMID 27122770. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4804823/. 
  36. ^ a b Mamoru Satoh; Kazunori Hirayoshi; Shinichi Yokota; Nobuko Hosokawa; Kazuhiro Nagata (1996-4-2). “Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen.”. Journal of Cell Biology 133: 469–83. doi:10.1083/jcb.133.2.469. PMC 2120794. PMID 8609177. https://doi.org/10.1083/jcb.133.2.469. 
  37. ^ Shinsuke Saga; Kazuhiro Nagata; Wen-Tien Chen; Kenneth M. Yamada (1987-7-1). “pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein.”. Journal of Cell Biology 105: 517–27. doi:10.1083/jcb.105.1.517. PMC 2114926. PMID 3038929. https://doi.org/10.1083/jcb.105.1.517. 
  38. ^ Hugh R. B. Pelham (1990-12). “The retention signal for soluble proteins of the endoplasmic reticulum”. Trends in Biochemical Sciences 15 (12): 483–6. doi:10.1016/0968-0004(90)90303-s. PMID 2077689. 
  39. ^ Christian Fork; Juliane Hitzel; Benjamin J Nichols; Ritva Tikkanen; Ralf P Brandes (2014-9-10). “Flotillin-1 facilitates toll-like receptor 3 signaling in human endothelial cells”. Basic Res. Cardiol (6): 439. doi:10.1007/s00395-014-0439-4. PMC 4330457. PMID 25204797. https://link.springer.com/article/10.1007/s00395-014-0439-4. 
  40. ^ a b “Molecular Weight - HSP47 | HSP47”. 2022年2月26日閲覧。
  41. ^ Alexandra Naba; Oliver M T Pearce; Amanda Del Rosario; Duanduan Ma; Huiming Ding; Vinothini Rajeeve; Pedro R Cutillas; Frances R Balkwill et al. (2017-8-4). “Characterization of the extracellular matrix of normal and diseased tissues using proteomics”. Journal of Proteome Research 16 (8): 3083–91. doi:10.1021/acs.jproteome.7b00191. PMC 8078728. PMID 28675934. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8078728/. 
  42. ^ Carla Hebert; Kathleen Norris; Ricardo Della Coletta; Mark Reynolds; José Ordóñez; John J. Sauk (1999-5-1). “Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines”. Journal of Cellular Biochemistry 73 (2): 248–58. doi:10.1002/(sici)1097-4644(19990501)73:2<248::aid-jcb11>3.0.co;2-a. PMID 10227388. 
  43. ^ Takako Hattori; Klaus von der Mark; Harumi Kawaki; Yasutaka Yutani; Satoshi Kubota; Tohru Nakanishi; Heidi Eberspaecher; Benoit de Crombrugghe et al. (2005-1). “Downregulation of rheumatoid arthritis-related antigen RA-A47 (HSP47/colligin-2) in chondrocytic cell lines induces apoptosis and cell-surface expression of RA-A47 in association with CD9”. Journal of Cellular Physiology 202 (1): 191–204. doi:10.1002/jcp.20112. PMID 15389525. 
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  45. ^ William J. Kaiser; Lisa-Marie Holbrook; Katherine L. Tucker; Ronald G. Stanley; Jonathan M. Gibbins (2009-6). “A functional proteomic method for the enrichment of peripheral membrane proteins reveals the collagen binding protein Hsp47 is exposed on the surface of activated human platelets”. Journal of Proteome Research 8 (6): 2903–14. doi:10.1021/pr900027j. PMID 19341245. 
  46. ^ 細胞表面につき、Ito and Nagata 2019
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  48. ^ 味呑憲二郎、新津洋司郎「HSP47 siRNAを用いた線維症治療薬の開発 ～ビタミン A 修飾リポソームによる星細胞標的化 DDS ～」『Drug Delivery System』第31巻第1号、日本DDS学会、2016年、62, 63、doi:10.2745/dds.31.62。 
  49. ^ Hiroko Masuda; Manabu Fukumoto; Kazunori Hirayoshi; Kazuhiro Nagata (1994-12-1). “Coexpression of the collagen-binding stress protein HSP47 gene and the alpha 1(I) and alpha 1(III) collagen genes in carbon tetrachloride-induced rat liver fibrosis”. Journal of Clinical Investigation (6): 2481–8. doi:10.1172/JCI117617. PMC 330081. PMID 7989606. https://doi.org/10.1172/JCI117617. 
  50. ^ 大塚健三. “HSP47はがん細胞の増殖や浸潤転移を促進する | 日本ハイパーサーミア学会”. 2022年1月7日閲覧。
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