The alpha v beta 3 "vitronectin receptor" is a member of the integrin superfamily of adhesion molecules. As such, this 160/85 kDa heterodimeric protein exhibits many of the typical structural and functional features of integrins. It mediates cell adhesion to extracellular matrix by recognizing the conserved arg-gly-asp (RGD) sequence of several plasma and matrix proteins. Recently, it has also been shown that alpha v beta 3 is involved in signal transduction and cell to cell interactions. alpha v beta 3 is highly expressed in bone resorbing cells, osteoclasts, and upregulated in response to vascular damage, during angiogenesis and in certain types of malignancy. Antagonists of alpha v beta 3 are being developed for use in a variety of diseases associated with altered receptor function or level.