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pubmed-article:2457583pubmed:abstractTextBinding of ligands that contain Arg-Gly-Asp to adhesion receptors induces cell spreading and aggregation and alters gene expression, possibly due to conformational changes within occupied adhesion receptors. PMI-1 is a monoclonal antibody which reacts with the platelet fibrinogen receptor, glycoprotein IIb-IIIa, and reports such a conformational change. ADP stimulation of platelets results in a fibrinogen-dependent increase in binding of the PMI-1 antibody. Peptides containing Arg-Gly-Asp also reversibly increase the binding of this antibody to cells and to purified glycoprotein IIb-IIIa. The PMI-1 antibody inhibits platelet adhesion and spreading on certain substrata (Shadle, P. J., Ginsberg, M. H., Plow, E. F., and Barondes, S. H. (1984) J. Cell Biol. 99, 2056-2060); thus this occupancy-modulated site may participate in adhesive function.lld:pubmed
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pubmed-article:2457583pubmed:articleTitleOccupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion.lld:pubmed
pubmed-article:2457583pubmed:affiliationDepartment of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.lld:pubmed
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