ADAMTS1ADAMTS20

ADAMTS1 and ADAMTS20 are two members of the ADAMTS (A disintegrin-like and metalloproteinase with thrombospondin motifs) gene family. Proteins in this family are secreted zinc-dependent metalloproteases that participate in extracellular matrix remodeling, tissue morphogenesis, and angiogenesis. ADAMTS1 and ADAMTS20 share a common domain organization, typically including a signal peptide for secretion, a pro-domain, a catalytic metalloprotease domain with the zinc-binding motif, a disintegrin-like domain, and one or more thrombospondin type 1 repeats. Activation usually involves removal of the pro-domain, enabling proteolytic activity in the extracellular milieu.

ADAMTS1 is among the better characterized members of the family. It participates in processing ECM components and can influence angiogenesis, with evidence that it modulates angiogenic processes in various tissues and pathological contexts. In addition to its proteolytic activities, ADAMTS1 has been studied for its roles in development, tissue remodeling, and cancer, where expression levels can affect tumor growth and vascularization. Its substrate range includes proteoglycans and other ECM constituents, contributing to matrix turnover and signaling landscapes.

ADAMTS20 is less extensively characterized relative to ADAMTS1 but is recognized as a developmentally important protease in several tissues. Expression patterns suggest involvement in organogenesis and tissue maturation, with functional data indicating roles in developmental processes that rely on ECM remodeling. Specific substrates and physiological contexts for ADAMTS20 continue to be explored, and research aims to clarify how it overlaps or diverges from other ADAMTS proteases.

Together, ADAMTS1 and ADAMTS20 illustrate the functional diversity of the ADAMTS family, balancing ECM degradation with modulation of signaling environments during development, tissue repair, and disease.