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Heat shock protein 47

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SERPINH1
Identifiers
AliasesSERPINH1, AsTP3, CBP1, CBP2, HSP47, OI10, PIG14, PPROM, RA-A47, SERPINH2, gp46, serpin family H member 1
External IDsOMIM: 600943; MGI: 88283; HomoloGene: 20331; GeneCards: SERPINH1; OMA:SERPINH1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

871

12406

Ensembl

ENSG00000149257

ENSMUSG00000070436

UniProt

P50454

P19324

RefSeq (mRNA)

NM_001207014
NM_001235

NM_001111043
NM_001111044
NM_009825
NM_001285776

RefSeq (protein)

NP_001193943
NP_001226

NP_001104513
NP_001104514
NP_001272705
NP_033955

Location (UCSC)Chr 11: 75.56 – 75.57 MbChr 7: 98.99 – 99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 by cells present in 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. Autoantibodies to this protein have been found in patients with rheumatoid arthritis.[5]

Interactions

Heat shock protein 47 has been shown to interact with collagens I, II, III, IV and V.[8]

References

  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:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)".
  6. ^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  7. ^ Williams, R. Sanders (21 March 2000). "Heat Shock Protein 47: A Chaperone for the Fibrous Cap?". Circulation. American Heart Association Inc. pp. 1227–1228. doi:10.1161/01.CIR.101.11.1227. Retrieved 11 December 2017.
  8. ^ 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.

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. 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, Tetuya Y, 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.
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • 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.
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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