Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion.

作者：Andrew L. Frelinger, S C Lam, Edward F. Plow, M. A. Smith, Joseph C. Loftus, Mark H. Ginsberg · 发表于：Journal of Biological Chemistry · 年份：1988 · DOI：10.1016/s0021-9258(18)37769-x · 被引用次数：277 · 研究领域：Cell Adhesion Molecules Research、Monoclonal and Polyclonal Antibodies Research、Platelet Disorders and Treatments

Binding 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.