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Target intelligence / Profile preview
Heat Shock Protein 47 (HSP47)
- Target
- HSP47
- Molecular classification
- Serine protease inhibitor, Molecular chaperone
01
Overview
Heat shock protein 47 (HSP47), also known as SERPINH1, is a collagen-specific molecular chaperone primarily located in the endoplasmic reticulum of collagen-producing cells. It plays a critical role in the biosynthesis, folding, assembly, and secretion of various types of collagens (notably types I–V). HSP47 is unique among heat shock proteins for its strict substrate specificity: it binds only to procollagen and collagen triple helices. It is implicated in fibrosis, cancer, and cardiovascular disease, making it a potential therapeutic target.
- Other names
- SERPINH1
02
Mechanism of action
Inhibition of HSP47 reduces collagen deposition and tumor progression
03
Biological functions
Collagen foldingCollagen assemblyProtein quality controlChaperone activity
04
Disease associations
FibrosisCancerCardiovascular diseaseDeep vein thrombosis
05
Safety considerations
Knockout models show embryonic lethality due to defective collagen biosynthesisPotential off-target effects on normal collagen homeostasis
06
Biomarkers
HSP47 expression levels correlate with fibrosis severityHSP47 expression levels correlate with tumor stage and aggressiveness
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