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

H. D. Gresham, J. L. Goodwin, P. M. Allen, D. C. Anderson, E. J. Brown

Research output: Contribution to journalArticlepeer-review

192 Scopus citations

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.

Original languageEnglish
Pages (from-to)1935-1943
Number of pages9
JournalJournal of Cell Biology
Volume108
Issue number5
DOIs
StatePublished - 1989

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