A disintegrin and metalloproteinase with thrombospondin motifs 10 (ADAMTS10)

A disintegrin and metalloproteinase with thrombospondin motifs 10 (ADAMTS10) is a secreted, zinc-dependent metalloprotease belonging to the ADAMTS family, characterized by thrombospondin type 1 repeats and a reprolysin-type metalloproteinase domain[3][4][7]. ADAMTS10 plays a crucial role in the assembly and organization of the extracellular matrix (ECM), particularly by regulating microfibril biogenesis via interaction with fibrillin-1, which is essential for connective tissue integrity[3]. It is widely expressed in many tissues and is critical during both prenatal and postnatal development, notably in the skin, eyes (lens), skeleton, and heart[1][2][4]. Loss-of-function defects in ADAMTS10 disrupt skeletal and ocular development and are causative for autosomal recessive Weill-Marchesani syndrome, a disorder marked by short stature, brachydactyly, stiff joints, and ocular abnormalities such as lens dislocation[2][4][5][6]. To date, there are no known small-molecule drugs or biologics that specifically target ADAMTS10, and its mechanism has not been exploited directly for therapeutic intervention. However, ADAMTS10 gene mutations serve as biomarkers for genetic disorders involving connective tissue abnormalities[2][4][7].

Other names

ADAM metallopeptidase with thrombospondin type 1 motif 10ADAM-TS10ADAMTS-10ATS10_HUMANa disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 10a disintegrin-like and metalloprotease domain with thrombospondin type I repeats 10