Abstract
The vitronectin receptor is a member of the integrin family of adhesion protein receptors and binds a broad spectrum of ligands, including fibronectin and fibrinogen in addition to vitronectin. We have generated four mAbs that recognize the murine alpha v beta 3 vitronectin receptor. Biochemical and expression analyses showed that two of the mAbs are specific for the alpha v chain, and two are specific for the beta 3 chain. The mAbs are effective blocking reagents and inhibited cell adhesion to vitronectin, fibrinogen, and fibronectin. Staining analysis revealed expression of alpha v and beta 3 on certain populations of murine thymocytes, splenocytes, and bone marrow cells. The expression of alpha v and beta 3 appeared to be modulated at specific stages of thymocyte development, suggesting a possible function for the alpha v beta 3 vitronectin receptor in T cell development.