Abstract
Abstract We report the identification of a 65-k Da lamininbinding protein (LBP) on the basal cell surface of embryonic corneal epithelium in chicken. The 65-k Da LBP was isolated by affinity chromatography with laminin-Sepharose. When reconstituted with lipid vesicles, it demonstrated specific binding for laminin. We produced monoclonal antibodies (MAbs) against 65-k Da LBP; these MAbs immuno-histochemically localized to the basal epithelial cell surface. One MAb interfered with the binding of laminin to isolated epithelia and purified 65-k Da LBP. It appears that we have identified, at least in part, a cell-surface binding site for laminin. This site would provide the important link between the extracellular laminin and the intracellular cytoskeleton, and potentially the metabolic machinery of the corneal epithelial cell.
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