TY - JOUR
T1 - A novel member of the integrin receptor family mediates Arg-Gly-Asp-stimulated neutrophil phagocytosis
AU - Gresham, H. D.
AU - Goodwin, J. L.
AU - Allen, P. M.
AU - Anderson, D. C.
AU - Brown, E. J.
PY - 1989
Y1 - 1989
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024506758&partnerID=8YFLogxK
U2 - 10.1083/jcb.108.5.1935
DO - 10.1083/jcb.108.5.1935
M3 - Article
C2 - 2785522
AN - SCOPUS:0024506758
SN - 0021-9525
VL - 108
SP - 1935
EP - 1943
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 5
ER -