ADAM15 peptidase (or metargidin; MEROPS identifier M12.215) is a sheddase-like metalloendopeptidase with a propeptide, a metallopeptidase domain, a disintegrin domain, an ADAM-CR domain, a transmembrane region and a proline-rich cytoplasmic tail. It probably exists naturally in a heterodimer with an unidentified, 56kDa protein with which it immunoprecipitates []. The precursor is correctly processed by furin []. ADAM15 sheds the ectodomain of fibroblast growth factor 2iiib []. In human (but not mouse) the disintegrin domain contains an RGD motif and binding to integrins has been demonstrated []. Because platelets bind to ADAM15 and are activated, clotting can occur, and ADAM15 is a therapeutic target for cardiovascular disease []. The gene is overexpressed in several human cancers and has roles in pathological neovascularization and prostate cancer metastasis []. A shorter spliced form with a different cytoplasmic tail containing an Src-binding site has been isolated from cancer cells [, ].
