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A Novel Member of the Integrin Receptor Family Mediates Arg-Gly-Asp-Stimulated Neutrophil Phagocytosis

Hattie D. Gresham, Jennifer L. Goodwin, Paul M. Allen, Donald C. Anderson and Eric J. Brown
The Journal of Cell Biology
Vol. 108, No. 5 (May, 1989), pp. 1935-1943
Stable URL: http://www.jstor.org/stable/1613447
Page Count: 9
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A Novel Member of the Integrin Receptor Family Mediates Arg-Gly-Asp-Stimulated Neutrophil Phagocytosis
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Abstract

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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