Serpin peptidase inhibitor, clade H (heat shock protein 47), member 1 (SERPINH1)

SERPINH1 encodes a collagen-specific molecular chaperone also known as heat shock protein 47 (HSP47), localized in the endoplasmic reticulum, and essential for the correct folding, maturation, and secretion of procollagen molecules. As a non-inhibitory member of the serpin family, it binds specifically to the triple-helical conformation of collagen, preventing aggregation and ensuring quality control during biosynthesis. SERPINH1 is upregulated in response to cellular stress (heat shock) and is induced in fibrotic, inflammatory, and neoplastic conditions. Dysregulation or mutation of SERPINH1 contributes to a variety of disease states including fibrosis, osteogenesis imperfecta, certain cancers, and autoimmune disease. Its central role in extracellular matrix remodeling makes it a potential target and biomarker in fibrotic disorders and cancer, but therapeutic targeting poses challenges due to its fundamental function in normal tissue homeostasis[1][2][3][4][5][7].

Other names

Serpin H1CBP1CBP2HSP47Colligin47 kDa heat shock proteinAsTP3PIG14Cell proliferation-inducing gene 14 proteinCollagen-binding protein 1Colligen-1Heat shock protein 47Rheumatoid arthritis-related antigen RA-A47OI10PPROMSERPINH2gp46Rheumatoid arthritis antigen A-47Serpin (or cysteine) proteinase inhibitor clade H member 1Collagen-binding protein 2Arsenic-transactivated protein 3

Inhibition of HSP47/SERPINH1 disrupts collagen folding and secretion, leading to reduced collagen deposition and fibrosis; potential anti-tumor effects via microenvironment modulation[5][4].