PECAM-1 (CD31) Cloning and Relation to Adhesion Molecules of the Immunoglobulin Gene Superfamily
Peter J. Newman, Michael C. Berndt, Jack Gorski, Gilbert White, Suzanne Lyman, Cathy Paddock, William A. Müller
Abstract
Peter J. Newman, Michael C. Berndt, Jack Gorski, Gilbert White, Suzanne Lyman, Cathy Paddock, William A. Müller
Abstract
An antibody to a platelet integral membrane glycoprotein was found to cross-react with the previously identified CD31 myelomonocytic differentiation antigen and with hec7, an endothelial cell protein that is enriched at intercellular junctions. This antibody identified a complementary DNA clone from an endothelial cell library. The 130-kilodalton translated sequence contained six extracellular immunoglobulin (Ig)-like domains and was most similar to the cell adhesion molecule (CAM) subgroup of the Ig superfamily. This is the only known member of the CAM family on platelets. Its cell surface distribution suggests participation in cellular recognition events.
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An antibody to a platelet integral membrane glycoprotein was found to cross-react with the previously identified CD31 myelomonocytic differentiation antigen and with hec7, an endothelial cell protein that is enriched at intercellular junctions. This antibody identified a complementary DNA clone from an endothelial cell library. The 130-kilodalton translated sequence contained six extracellular immunoglobulin (Ig)-like domains and was most similar to the cell adhesion molecule (CAM) subgroup of the Ig superfamily. This is the only known member of the CAM family on platelets. Its cell surface distribution suggests participation in cellular recognition events.
Key concepts: Immunoglobulin superfamily, Immunoglobulin domain, Immunoglobulin gene, Antibody, Cell adhesion molecule, Biology, Glycoprotein, Cell adhesion