The IIb-IIIa glycoprotein complex that mediates platelet aggregation is directly implicated in leukocyte adhesion

Cell. 1986 Apr 25;45(2):269-80. doi: 10.1016/0092-8674(86)90391-0.

Abstract

Evidence is presented that the IIb-IIIa glycoprotein complex, which functions as the receptor for fibrinogen on platelets and is central to platelet aggregation, is expressed on the surface of leukocytes where it may function as a receptor for fibronectin. F(ab')2 fragments of a monoclonal antibody, 25E11, raised against activated large granular lymphocytes, inhibited killing by natural killer cells, blocked the binding of fibronectin-coated particles by monocytes, and stimulated neutrophils to exhibit increased antibody-dependent killing. Immunoprecipitation studies of leukocytes and platelets, and the ability of 25E11 to inhibit platelet aggregation, identified the antigen as an epitope on the IIb-IIIa complex. This glycoprotein thus constitutes the first example of a receptor mediating both platelet aggregation and leukocyte adhesion.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adult
  • Antibodies, Monoclonal / immunology
  • Cell Adhesion*
  • Child
  • Cytotoxicity, Immunologic
  • Epitopes / immunology
  • Fibronectins / metabolism
  • Humans
  • Immunoglobulin Fab Fragments / immunology
  • Killer Cells, Natural / immunology
  • Leukocytes / cytology*
  • Platelet Aggregation*
  • Platelet Membrane Glycoproteins
  • Receptors, Cell Surface / physiology*
  • Receptors, Fibronectin
  • Receptors, Immunologic / metabolism
  • Thrombasthenia / immunology
  • Thrombasthenia / pathology

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • Fibronectins
  • Immunoglobulin Fab Fragments
  • Platelet Membrane Glycoproteins
  • Receptors, Cell Surface
  • Receptors, Fibronectin
  • Receptors, Immunologic