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SERPINH1
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; OMA:SERPINH1 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	75,572,783 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	99,002,446 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; smooth muscle tissue; ; pericardium; ; right coronary artery; ; ascending aorta; ; left uterine tube; ; cartilage tissue; ; body of uterus; ; right ovary; ; upper lobe of left lung;
	Top expressed in
	dermis; ; molar; ; ascending aorta; ; calvaria; ; aortic valve; ; atrium; ; body of femur; ; umbilical cord; ; hand; ; maxillary prominence;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	unfolded protein binding; collagen binding; RNA binding; serine-type endopeptidase inhibitor activity;
Cellular component	cytoplasm; membrane raft; endoplasmic reticulum lumen; extracellular exosome; endoplasmic reticulum-Golgi intermediate compartment; extracellular space; endoplasmic reticulum; collagen-containing extracellular matrix;
Biological process	response to unfolded protein; protein maturation; chondrocyte development involved in endochondral bone morphogenesis; collagen biosynthetic process; collagen fibril organization; negative regulation of endopeptidase activity;
	Sources:Amigo / QuickGO
Orthologs
	871
	12406
	ENSG00000149257
	ENSMUSG00000070436
	P50454
	P19324
	NM_001207014; NM_001235
	NM_001111043; NM_001111044; NM_009825; NM_001285776
	NP_001193943; NP_001226
	NP_001104513; NP_001104514; NP_001272705; NP_033955
	Wikidata
View/Edit Human	View/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 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. Antibodies directed 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 RS (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, Baumann U (2013-01-09). "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 (33): 13243–13247. doi:10.2210/pdb3zha/pdb. PMC 3421173. PMID 22847422. 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 B, Balamurugan K (2020), "Role of Heat Shock Factors in Diseases and Immunity", Heat Shock Proteins in Human Diseases, Cham: Springer International Publishing, pp. 197–210, doi:10.1007/7515_2020_21, ISBN 978-3-030-62288-6, S2CID 226465376, retrieved 2023-11-26
^ Kim HJ, Park JH, Shin JM, Yang HW, Lee HM, Park IH (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): 9585. Bibcode:2020NatSR..10.9585K. doi:10.1038/s41598-020-66547-z. ISSN 2045-2322. PMC 7280506. PMID 32514115.
^ Sakamoto N, Okuno D, Tokito T, Yura H, Kido T, Ishimoto H, Tanaka Y, Mukae H (2023-08-25). "HSP47: A Therapeutic Target in Pulmonary Fibrosis". Biomedicines. 11 (9): 2387. doi:10.3390/biomedicines11092387. ISSN 2227-9059. PMC 10525413. PMID 37760828.

External links

The MEROPS online database for peptidases and their inhibitors: I04.035 Archived 2012-12-23 at archive.today
HSP47+Heat-Shock+Proteins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)