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Serpin H1 (None)

Target: None
Molecular classification: Serpin, Molecular chaperone

Overview

Serpin H1 (SERPINH1), also known as Heat Shock Protein 47 (HSP47), is a member of the serpin superfamily and functions as a collagen-specific molecular chaperone. It is essential for the correct folding and maturation of procollagen molecules within the endoplasmic reticulum. Aberrant expression is associated with various cancers and other diseases such as rheumatoid arthritis and preterm birth, making it a potential biomarker and therapeutic target.

Other names: HSP47AsTP3CBP1CBP2OI10PIG14PPROMRA-A47SERPINH2gp46Heat Shock Protein 47

Mechanism of action

Inhibition of collagen misfolding and aggregation, regulation of protease activity

Biological functions

Collagen biosynthesisProtease homeostasisProtein foldingExtracellular matrix organizationImmune response modulation

Disease associations

Cancer progressionRheumatoid arthritisPreterm birthTumor progression

Biomarkers

SERPINH1 expression levels (prognostic biomarker in various cancers)

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