Abstract
Background: ADAM (a disintegrin and metalloprotease) family is important in diverse biologic processes such as cell adhesion and proteolytic shedding of cell surface receptors. Human ADAM15 (named metargidin) is the only one that has an argininel-glycine-aspartic acid (RGD) integrin-binding motif. However, the mouse and rat orthologues of ADAM15 lack an RGD sequence, but mouse ADAM15 can bind integrin α9β1. ADAM15 is strongly expressed in endothelial cell. Over expression ADAM15 showed to enhance cell-cell interaction and reduce cell migration. ADAM15-/- mice showed a 64% reduced neovascularization in an oxygen induced model of proliferative retinopathy. ADAM9-/- and ADAM9, 15-/- double knockout increase pathological neovascularization. However, the role of ADAM9 and 15 in angiogenesis is still unknown.
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