ADAM metallopeptidase with thrombospondin type 1 motif 2 (ADAMTS2)

ADAM metallopeptidase with thrombospondin type 1 motif 2 (ADAMTS2) is an enzyme belonging to the ADAMTS protein family, characterized by disintegrin and metallopeptidase activity along with thrombospondin type 1 motifs[1][2][3][4][5][6]. ADAMTS2 is responsible for the proteolytic excision of the N-terminal propeptide from fibrillar procollagen types I, II, and V, a critical step in collagen fibril maturation and extracellular matrix formation[1][5]. Mutations in the ADAMTS2 gene are causative for dermatosparaxis type Ehlers-Danlos syndrome (type VIIC), a connective tissue disorder characterized by extreme skin fragility and laxity[1][2]. ADAMTS2 plays a fundamental role in connective tissue biology, with potential involvement in additional connective tissue diseases[1][2][5]. No approved therapeutics directly target ADAMTS2, but its biological role makes it a potential target of interest in fibrosis and tissue remodeling research.

Other names

ADAMTS2ADAM-TS2ADAMTS-3PCINPProcollagen N-endopeptidaseProcollagen I N-proteinaseNPIA disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 2A disintegrin and metalloproteinase with thrombospondin motifs 2Procollagen I/II amino propeptide-processing enzyme

Proteolytic cleavage of the N-propeptide of fibrillar procollagens (types I, II, V); Enzymatic modification of extracellular matrix proteins; Inhibition or modulation would alter collagen maturation and extracellular matrix structure