Distintegrin and Metalloproteinase (ADAM)
ADAM proteins are members of the same superfamily as MMPs, namely the Metzincins, named for their zinc binding domains and their structurally important C-terminal conserved methionine residue. The name ADAM stands for “A Disintegrin And Metalloprotease” and like the name suggests, ADAM proteins are cell surface proteins that possess both an adhesion domain as well as a protease domain (Wolfsberg, TG et al. J Cell Biol 1995; 131:275–278).
There are more than 35 members of the ADAM family of proteins; the precise function of many the ADAM family members are unknown, but some, such as ADAM17 (a.k.a. tumor necrosis factor–a converting enzyme) have known biological functions. An additional class of ADAM related proteins are known as the ADAMTS proteins. ADAMTS proteins are structurally homologous to ADAM proteins, but they contain at least one C-terminal thrombospondin type 1 (TSP1) repeat and are secreted rather than membrane bound. ADAMTS1 and ADAMTS8 are inhibitors of angiogenesis, and others, such as ADAMTS5, cleave extracellular proteoglycans such as aggrecan.
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