A novel member of the integrin receptor family mediates Arg-Gly-Asp-stimulated neutrophil phagocytosis.
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.
Gresham
H D
HD
Department of Medicine, Washington University, St. Louis, Missouri 63110.
Goodwin
J L
JL
Allen
P M
PM
Anderson
D C
DC
Brown
E J
EJ
D000595:Amino Acid Sequence; D001792:Blood Platelets / Q000276:immunology; D002374:Catalase / Q000494:pharmacology; D002462:Cell Membrane / Q000276:immunology; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D016023:Integrins; D007700:Kinetics; D008562:Membrane Glycoproteins / Q000502:physiology*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000187:drug effects / Q000276:immunology / Q000502:physiology*; D009842:Oligopeptides / Q000494:pharmacology*; D010587:Phagocytosis / Q000187:drug effects*; D010920:Placenta / Q000276:immunology; D011247:Pregnancy; D011971:Receptors, Immunologic / Q000502:physiology*
D016023:Integrins; D008562:Membrane Glycoproteins; D009842:Oligopeptides; D011971:Receptors, Immunologic; C047981:arginyl-glycyl-aspartic acid; D002374:Catalase