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

A. L. Frelinger, S. C.T. Lam, E. F. Plow, M. A. Smith, J. C. Loftus, M. H. Ginsberg

Research output: Contribution to journalArticle

204 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)12397-12402
Number of pages6
JournalJournal of Biological Chemistry
Volume263
Issue number25
StatePublished - Dec 1 1988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Frelinger, A. L., Lam, S. C. T., Plow, E. F., Smith, M. A., Loftus, J. C., & Ginsberg, M. H. (1988). Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion. Journal of Biological Chemistry, 263(25), 12397-12402.