Cell-matrix interactions play a fundamental role in normal and pathological conditions. They can be mediated by the cytoadhesin subgroup of the integrin superfamily of adhesion molecules. Its members include the vitronectin receptor (VNR) and the platelet glycoprotein IIb/IIIa (GP IIb/IIIa). Both receptors are composed of an alpha-chain (alpha(v), and alpha(IIb), respectively) coupled to a beta-3-chain. Using in situ immunohistochemistry and monoclonal antibodies, the authors studied the distribution of GP IIIa (common-beta-3-chain), GP IIb/IIIa (alpha(IIb-chain)) and VNR (alpha(v)-chain) in normal and pathological corneal tissues. In the normal cornea, the limbal vascular endothelium was weakly alpha(v)-positive. Occasionally, faint and granular staining was seen in the epithelium. In the pathological samples, an upregulated expression of the alpha(v)-chain was noticed on the corneal epithelium as well as on fibroblasts and corneal endothelium. The alpha(IIb) and beta-3-chains were consistently absent. These data suggest that expression of the VNR-alpha(v)-chain in the human cornea is modulated by soluble factors released during inflammation and wound healing. Dissociation of expression of the alpha(v), and beta-3-chains suggests usage of an alternative beta-chain by the VNR-alpha(v)-chain.