A novel member of the integrin receptor family mediates Arg-Gly-Asp- stimulated neutrophil phagocytosis

doi:10.1083/jcb.108.5.1935

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A novel member of the integrin receptor family mediates Arg-Gly-Asp- stimulated neutrophil phagocytosis

HD Gresham, JL Goodwin, PM Allen, DC Anderson and EJ Brown
Department of Medicine, Washington University, St. Louis, Missouri 63110.

Human neutrophils (PMN) express a heterodimeric receptor that has ligand binding specificity for the Arg-Gly-Asp (RGD) sequence within many adhesive proteins. A monoclonal antibody, B6H12, which binds to this receptor, inhibits both RGD-mediated ligand binding and stimulation of IgG-mediated phagocytosis by fibronectin, fibrinogen, vitronectin, von Willebrand's factor, and collagen type IV. By several criteria this receptor is neither a known very late antigen, a known cytoadhesin (gp IIb/IIIa-vitronectin receptor), nor a member of the LFA- 1, Mac-1, p150,95 group of integrin receptors. Ligand binding via this receptor is rapidly inactivated by products of the myeloperoxidase- hydrogen peroxide-halide system of PMN. We conclude that this receptor, for which we propose the name leukocyte response integrin, is a signal- transducing molecule on PMN which may have a significant early role in modulation of PMN function at inflammatory sites.
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