ADAMTS10

ADAMTS10 is a member of the ADAMTS family of secreted zinc-dependent metalloproteases, enzymes that participate in extracellular matrix remodeling. The protein is synthesized with a signal peptide and a propeptide that is typically cleaved to activate the enzyme. It contains a metalloprotease catalytic domain, a disintegrin-like domain, a spacer region, and thrombospondin type 1 repeats, reflecting the characteristic architecture of ADAMTS proteins. As a secreted extracellular protease, ADAMTS10 functions outside the cell in the ECM.

The precise in vivo substrates of ADAMTS10 are not fully defined, but the protein is thought to participate in the assembly and turnover of extracellular matrix components, including microfibrils and proteoglycans. Through these activities, it is involved in tissue organization and development. Expression studies show ADAMTS10 in multiple tissues, with patterns suggesting roles in connective tissues and in ocular, skeletal, and developmental contexts. Its activity may influence the integrity of ECM networks and the formation of microfibrils.

In humans, variants in ADAMTS10 have been described in association with inherited disorders affecting connective tissue and ocular tissues, and research in model systems continues to explore the mechanisms by which altered ADAMTS10 function disrupts ECM organization. The gene is conserved across vertebrates, underscoring an essential role in ECM dynamics. Ongoing investigations aim to identify specific substrates, regulatory factors, and the range of phenotypes linked to ADAMTS10 mutations.