Disintegrin and metalloproteinase domain-containing protein 15 (ADAM15)

Disintegrin and metalloproteinase domain-containing protein 15 (ADAM15) is a transmembrane enzyme of the ADAM family, characterized by multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like RGD motif for integrin binding, an EGF-like domain, and a cysteine-rich domain. ADAM15 participates in cell adhesion, migration, proteolytic cleavage of membrane proteins (shedding), and is involved in several signaling pathways. Its unique RGD motif mediates specific integrin interactions, and the protein significantly affects cellular processes such as wound healing, inflammation, angiogenesis, and apoptosis resistance. Overexpression or dysregulation of ADAM15 is implicated in the pathogenesis and progression of various diseases, most notably cancers and inflammatory conditions, making it a potential but challenging therapeutic target due to family-wide redundancy and complex biological roles[1][2][3][4][6].

Other names

ADAM metallopeptidase domain 15ADAM 15MDC15MDC-15MetargidinMetalloprotease RGD disintegrin protein

Protease inhibitors: Block metalloprotease activity, preventing substrate cleavage (possible, based on the enzyme family)[1][6]. Integrin antagonists: Can disrupt ADAM15's engagement of integrins through its RGD motif[4]. Targeting splice variants or cytoplasmic interaction domains could influence cell signaling pathways, but no approved drugs currently use these mechanisms[2][3].