ADAM metallopeptidase with thrombospondin type 1 motif 17 (ADAMTS17)

ADAM metallopeptidase with thrombospondin type 1 motif 17 (ADAMTS17) is a secreted member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family of metalloproteinases[1][4]. It plays a critical role in the formation, maintenance, and modulation of extracellular microfibril networks, especially in ocular zonules and connective tissues[1][2]. ADAMTS17 regulates the balance and incorporation of fibrillin isoforms in microfibrils, influencing extracellular matrix integrity and skeletal development[1][2]. Loss-of-function mutations in ADAMTS17 cause Weill–Marchesani syndrome (WMS) and related disorders, leading to features such as ocular anomalies (ectopia lentis, high myopia), short stature, spherophakia, and sometimes glaucoma[1][3][4]. At the molecular level, ADAMTS17 interacts with fibrillin-2 but not fibrillin-1, and does not cleave either molecule; instead, it suppresses fibrillin-2 incorporation into microfibrils in part by transcriptionally downregulating FBN2 expression[2][3]. It also modulates the BMP-Smad 1/5/8 signaling pathway and is thought to be crucial for proper skeletal formation and growth plate function[3]. ADAMTS17’s primary disease relevance is as a genetic determinant in connective tissue syndromes; no therapeutically approved drugs are known to target this protein directly.

Other names

A disintegrin and metalloproteinase with thrombospondin motifs 17ADAM-TS 17ADAM-TS17ADAMTS-17FLJ32769FLJ16363WMS4