Heat shock protein 47

Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen.[5][6]

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
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

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. 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]

Research on role in preventing deep vein thrombosis

Research published in 2023 indicates a potential role of HSP47 regarding deep vein thrombosis.[9] [10] This initial research will be followed by additional studies.

References

  1. GRCh38: Ensembl release 89: ENSG00000149257 - Ensembl, May 2017
  2. 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. "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.
  7. 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.
  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.
  9. Schattner, Mirta, Sleep like a bear, Science, April 13, 2023
  10. Garcia de Jesús, Erin, Hibernating bears don’t get blood clots. Now scientists know why, Science News, April 13, 2023

Further reading

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