Heat shock protein 47: Difference between revisions
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Added information on the structure, added more information on interactions and research on the role of HSP47 in fibrosis. |
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== Function == |
== Function == |
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This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is expressed in the endoplasmic reticulum. These cells synthesize and secrete type I and type II collagen. <ref>{{cite journal|last1=Williams|first1=R. Sanders|title=Heat Shock Protein 47: A Chaperone for the Fibrous Cap?|url=http://circ.ahajournals.org/content/101/11/1227.full|journal=Circulation|volume=101|issue=11|access-date=11 December 2017|pages=1227–1228|language=en|doi=10.1161/01.CIR.101.11.1227|date=21 March 2000|pmid=10725278|doi-access=free}}</ref> The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. |
This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is expressed in the endoplasmic reticulum. These cells synthesize and secrete type I and type II collagen. <ref>{{cite journal|last1=Williams|first1=R. Sanders|title=Heat Shock Protein 47: A Chaperone for the Fibrous Cap?|url=http://circ.ahajournals.org/content/101/11/1227.full|journal=Circulation|volume=101|issue=11|access-date=11 December 2017|pages=1227–1228|language=en|doi=10.1161/01.CIR.101.11.1227|date=21 March 2000|pmid=10725278|doi-access=free}}</ref> The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. HSP47 is essential for the correct folding of procollagen. to this protein have been found in patients with rheumatoid arthritis.<ref name="entrez"/> |
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== Structure == |
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HSP47 contains 3 beta sheets and 9 alpha helices. After binding with collagen no conformation change is observed.<ref name=":0">{{Cite web |last=Widmer |first=C. |last2=Gebauer |first2=J.M. |last3=Baumann |first3=U. |date=2013-01-09 |title=Molecular basis for the action of the collagen-specific chaperone Hsp47 SERPINH1 and its structure-specific client recognition. |url=http://dx.doi.org/10.2210/pdb3zha/pdb |access-date=2023-11-26 |website=dx.doi.org}}</ref> |
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== Interactions == |
== Interactions == |
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Heat shock protein 47 has been shown to [[Protein-protein interaction|interact]] with collagens I, II, III, IV and V.<ref>{{cite journal | vauthors = Mala JG, Rose C | title = Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model? | journal = Life Sciences | volume = 87 | issue = 19–22 | pages = 579–86 | date = November 2010 | pmid = 20888348 | doi = 10.1016/j.lfs.2010.09.024 }}</ref> |
Heat shock protein 47 has been shown to [[Protein-protein interaction|interact]] with collagens I, II, III, IV and V.<ref>{{cite journal | vauthors = Mala JG, Rose C | title = Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model? | journal = Life Sciences | volume = 87 | issue = 19–22 | pages = 579–86 | date = November 2010 | pmid = 20888348 | doi = 10.1016/j.lfs.2010.09.024 }}</ref> It is involved in the secretion of collagen as well as the processing, assembly, and folding of collagen proteins. Hsp 47 binds specifically to procollagen and collagen only. The protein recognizes the triple helix of procollagen, two HSP47 proteins will bind to the leading and trailing strands of procollagen.<ref name=":0" /> |
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== Research on role in preventing deep vein thrombosis == |
== Research on role in preventing deep vein thrombosis == |
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Research published in 2023 indicates a potential role of HSP47 regarding [[deep vein thrombosis]].<ref>Schattner, Mirta, ''[https://www.science.org/doi/10.1126/science.adh3276 Sleep like a bear]'', [[Science (magazine)|Science]], April 13, 2023</ref> <ref>Garcia de Jesús, Erin, ''[https://www.sciencenews.org/article/hibernating-bears-blood-clots Hibernating bears don’t get blood clots. Now scientists know why]'', Science News, April 13, 2023</ref> This initial research will be followed by additional studies. |
Research published in 2023 indicates a potential role of HSP47 regarding [[deep vein thrombosis]].<ref>Schattner, Mirta, ''[https://www.science.org/doi/10.1126/science.adh3276 Sleep like a bear]'', [[Science (magazine)|Science]], April 13, 2023</ref> <ref>Garcia de Jesús, Erin, ''[https://www.sciencenews.org/article/hibernating-bears-blood-clots Hibernating bears don’t get blood clots. Now scientists know why]'', Science News, April 13, 2023</ref> This initial research will be followed by additional studies. |
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== Role in Fibrosis == |
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Fibrosis is the scarring of connective tissue, one attribute is the excess deposition of collagen in the extracellular matrix of tissue. Research has shown that HSPs have a role in fibrotic diseases.<ref>{{Citation |last=Balasubramaniam |first=Boopathi |title=Role of Heat Shock Factors in Diseases and Immunity |date=2020 |url=http://dx.doi.org/10.1007/7515_2020_21 |work=Heat Shock Proteins in Human Diseases |pages=197–210 |access-date=2023-11-26 |place=Cham |publisher=Springer International Publishing |isbn=978-3-030-62288-6 |last2=Balamurugan |first2=Krishnaswamy}}</ref> HSP47 has been shown to be pro-fibrosis in various fibrotic diseases. During the process of fibrosis, HSP47 is expressed and is involved in the production of collagen.<ref>{{Cite journal |last=Kim |first=Hae-Ji |last2=Park |first2=Joo-Hoo |last3=Shin |first3=Jae-Min |last4=Yang |first4=Hyun-Woo |last5=Lee |first5=Heung-Man |last6=Park |first6=Il-Ho |date=2020-06-09 |title=Author Correction: TGF-β1-induced HSP47 regulates extracellular matrix accumulation via Smad2/3 signaling pathways in nasal fibroblasts |url=http://dx.doi.org/10.1038/s41598-020-66547-z |journal=Scientific Reports |volume=10 |issue=1 |doi=10.1038/s41598-020-66547-z |issn=2045-2322}}</ref> HSP47 could be a potential therapeutic agent for fibrotic disease, a down-regulation of HSP47 leads to decreased fibrotic progression.<ref>{{Cite journal |last=Sakamoto |first=Noriho |last2=Okuno |first2=Daisuke |last3=Tokito |first3=Takatomo |last4=Yura |first4=Hirokazu |last5=Kido |first5=Takashi |last6=Ishimoto |first6=Hiroshi |last7=Tanaka |first7=Yoshimasa |last8=Mukae |first8=Hiroshi |date=2023-08-25 |title=HSP47: A Therapeutic Target in Pulmonary Fibrosis |url=http://dx.doi.org/10.3390/biomedicines11092387 |journal=Biomedicines |volume=11 |issue=9 |pages=2387 |doi=10.3390/biomedicines11092387 |issn=2227-9059}}</ref> |
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== References == |
== References == |
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Revision as of 01:31, 26 November 2023
| SERPINH1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | SERPINH1, AsTP3, CBP1, CBP2, HSP47, OI10, PIG14, PPROM, RA-A47, SERPINH2, gp46, serpin family H member 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 600943 MGI: 88283 HomoloGene: 20331 GeneCards: SERPINH1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen.[5][6]
Function
This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is expressed in the endoplasmic reticulum. These cells synthesize and secrete type I and type II collagen. [7] The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. HSP47 is essential for the correct folding of procollagen. to this protein have been found in patients with rheumatoid arthritis.[5]
Structure
HSP47 contains 3 beta sheets and 9 alpha helices. After binding with collagen no conformation change is observed.[8]
Interactions
Heat shock protein 47 has been shown to interact with collagens I, II, III, IV and V.[9] It is involved in the secretion of collagen as well as the processing, assembly, and folding of collagen proteins. Hsp 47 binds specifically to procollagen and collagen only. The protein recognizes the triple helix of procollagen, two HSP47 proteins will bind to the leading and trailing strands of procollagen.[8]
Research on role in preventing deep vein thrombosis
Research published in 2023 indicates a potential role of HSP47 regarding deep vein thrombosis.[10] [11] This initial research will be followed by additional studies.
Role in Fibrosis
Fibrosis is the scarring of connective tissue, one attribute is the excess deposition of collagen in the extracellular matrix of tissue. Research has shown that HSPs have a role in fibrotic diseases.[12] HSP47 has been shown to be pro-fibrosis in various fibrotic diseases. During the process of fibrosis, HSP47 is expressed and is involved in the production of collagen.[13] HSP47 could be a potential therapeutic agent for fibrotic disease, a down-regulation of HSP47 leads to decreased fibrotic progression.[14]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000149257 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000070436 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)".
- ^ Dafforn TR, Della M, Miller AD (December 2001). "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.
- ^ Williams, R. Sanders (21 March 2000). "Heat Shock Protein 47: A Chaperone for the Fibrous Cap?". Circulation. 101 (11): 1227–1228. doi:10.1161/01.CIR.101.11.1227. PMID 10725278. Retrieved 11 December 2017.
- ^ a b Widmer, C.; Gebauer, J.M.; Baumann, U. (2013-01-09). "Molecular basis for the action of the collagen-specific chaperone Hsp47 SERPINH1 and its structure-specific client recognition". dx.doi.org. Retrieved 2023-11-26.
- ^ Mala JG, Rose C (November 2010). "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.
- ^ Schattner, Mirta, Sleep like a bear, Science, April 13, 2023
- ^ Garcia de Jesús, Erin, Hibernating bears don’t get blood clots. Now scientists know why, Science News, April 13, 2023
- ^ Balasubramaniam, Boopathi; Balamurugan, Krishnaswamy (2020), "Role of Heat Shock Factors in Diseases and Immunity", Heat Shock Proteins in Human Diseases, Cham: Springer International Publishing, pp. 197–210, ISBN 978-3-030-62288-6, retrieved 2023-11-26
- ^ Kim, Hae-Ji; Park, Joo-Hoo; Shin, Jae-Min; Yang, Hyun-Woo; Lee, Heung-Man; Park, Il-Ho (2020-06-09). "Author Correction: TGF-β1-induced HSP47 regulates extracellular matrix accumulation via Smad2/3 signaling pathways in nasal fibroblasts". Scientific Reports. 10 (1). doi:10.1038/s41598-020-66547-z. ISSN 2045-2322.
- ^ Sakamoto, Noriho; Okuno, Daisuke; Tokito, Takatomo; Yura, Hirokazu; Kido, Takashi; Ishimoto, Hiroshi; Tanaka, Yoshimasa; Mukae, Hiroshi (2023-08-25). "HSP47: A Therapeutic Target in Pulmonary Fibrosis". Biomedicines. 11 (9): 2387. doi:10.3390/biomedicines11092387. ISSN 2227-9059.
{{cite journal}}: CS1 maint: unflagged free DOI (link)
Further reading
- Razzaque MS, Taguchi T (October 1999). "The possible role of colligin/HSP47, a collagen-binding protein, in the pathogenesis of human and experimental fibrotic diseases". Histology and Histopathology. 14 (4): 1199–212. PMID 10506936.
- Gettins PG (December 2002). "Serpin structure, mechanism, and function". Chemical Reviews. 102 (12): 4751–804. doi:10.1021/cr010170. PMID 12475206.
- Clarke EP, Sanwal BD (January 1992). "Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1129 (2): 246–8. doi:10.1016/0167-4781(92)90498-o. PMID 1309665.
- Ikegawa S, Sudo K, Okui K, Nakamura Y (1995). "Isolation, characterization and chromosomal assignment of human colligin-2 gene (CBP2)". Cytogenetics and Cell Genetics. 71 (2): 182–6. doi:10.1159/000134103. PMID 7656593.
- Ikegawa S, Nakamura Y (July 1997). "Structure of the gene encoding human colligin-2 (CBP2)". Gene. 194 (2): 301–3. doi:10.1016/S0378-1119(97)00209-6. PMID 9272875.
- Bekri S, Adélaïde J, Merscher S, Grosgeorge J, Caroli-Bosc F, Perucca-Lostanlen D, Kelley PM, Pébusque MJ, Theillet C, Birnbaum D, Gaudray P (1998). "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma". Cytogenetics and Cell Genetics. 79 (1–2): 125–31. doi:10.1159/000134699. PMID 9533029.
- Hattori T, Fujisawa T, Sasaki K, Yutani Y, Nakanishi T, Takahashi K, Takigawa M (April 1998). "Isolation and characterization of a rheumatoid arthritis-specific antigen (RA-A47) from a human chondrocytic cell line (HCS-2/8)". Biochemical and Biophysical Research Communications. 245 (3): 679–83. doi:10.1006/bbrc.1998.8505. PMID 9588174.
- Nagai N, Yorihuzi T, Hosokawa N, Nagata K (February 1999). "The human genome has only one functional hsp47 gene (CBP2) and a pseudogene (pshsp47)". Gene. 227 (2): 241–8. doi:10.1016/S0378-1119(98)00592-7. PMID 10023073.
- Hebert C, Norris K, Della Coletta R, Reynolds M, Ordóñez J, Sauk JJ (May 1999). "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. S2CID 41309881.
- Koide T, Aso A, Yorihuzi T, Nagata K (September 2000). "Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47". The Journal of Biological Chemistry. 275 (36): 27957–63. doi:10.1074/jbc.M003026200. PMID 10862616.
- Hattori T, Takahash K, Yutani Y, Fujisawa T, Nakanishi T, Takigawa M (2001). "Rheumatoid arthritis-related antigen 47kDa (RA-A47) is a product of colligin-2 and acts as a human HSP47". Journal of Bone and Mineral Metabolism. 18 (6): 328–34. doi:10.1007/s007740070004. PMID 11052465. S2CID 35696096.
- Pelletier G, Stefanovsky VY, Faubladier M, Hirschler-Laszkiewicz I, Savard J, Rothblum LI, Côté J, Moss T (November 2000). "Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription". Molecular Cell. 6 (5): 1059–66. doi:10.1016/S1097-2765(00)00104-0. PMID 11106745.
- Matsuda M, Koide T, Yorihuzi T, Hosokawa N, Nagata K (January 2001). "Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences". Biochemical and Biophysical Research Communications. 280 (2): 535–40. doi:10.1006/bbrc.2000.4149. PMID 11162551.
- Zhou M, Nekhai S, Bharucha DC, Kumar A, Ge H, Price DH, Egly JM, Brady JN (November 2001). "TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription". The Journal of Biological Chemistry. 276 (48): 44633–40. doi:10.1074/jbc.M107466200. PMID 11572868.
- Song CZ, Keller K, Murata K, Asano H, Stamatoyannopoulos G (March 2002). "Functional interaction between coactivators CBP/p300, PCAF, and transcription factor FKLF2". The Journal of Biological Chemistry. 277 (9): 7029–36. doi:10.1074/jbc.M108826200. PMC 2808425. PMID 11748222.
- Sasaki H, Sato T, Yamauchi N, Okamoto T, Kobayashi D, Iyama S, Kato J, Matsunaga T, Takimoto R, Takayama T, Kogawa K, Watanabe N, Niitsu Y (May 2002). "Induction of heat shock protein 47 synthesis by TGF-beta and IL-1 beta via enhancement of the heat shock element binding activity of heat shock transcription factor 1". Journal of Immunology. 168 (10): 5178–83. doi:10.4049/jimmunol.168.10.5178. PMID 11994473.
- Razzaque MS, Ahmed AR (March 2002). "Collagens, collagen-binding heat shock protein 47 and transforming growth factor-beta 1 are induced in cicatricial pemphigoid: possible role(s) in dermal fibrosis". Cytokine. 17 (6): 311–6. doi:10.1006/cyto.2002.1020. PMID 12061838.
- Sato K, Yomogida K, Wada T, Yorihuzi T, Nishimune Y, Hosokawa N, Nagata K (October 2002). "Type XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovary". The Journal of Biological Chemistry. 277 (40): 37678–84. doi:10.1074/jbc.M205347200. PMID 12145293.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Rocnik EF, van der Veer E, Cao H, Hegele RA, Pickering JG (October 2002). "Functional linkage between the endoplasmic reticulum protein Hsp47 and procollagen expression in human vascular smooth muscle cells". The Journal of Biological Chemistry. 277 (41): 38571–8. doi:10.1074/jbc.M206689200. PMID 12163502.
External links
- The MEROPS online database for peptidases and their inhibitors: I04.035
- HSP47+Heat-Shock+Proteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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