TY - JOUR
T1 - Integrin-associated protein
T2 - A 50-kD plasma membrane antigen physically and functionally associated with integrins
AU - Brown, Eric
AU - Hooper, Lora
AU - Ho, Thang
AU - Gresham, Hattie
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1990
Y1 - 1990
N2 - Phagocytosis by monocytes or neutrophils can be enhanced by interaction with several proteins or synthetic peptides containing the Arg-Gly-Asp sequence. Recently we showed that an mAb, B6H12, specifically inhibited this enhancement of neutrophi1 phagocytosis by inhibiting Arg-Gly-Asp binding to the leukocyte response integrin (Gresham, H.D., J.L. Goodwin, P.M. Allen, D.C. Anderson, and E.J. Brown. 1989. J. Cell Biol. 108:1935-1943). Now, we have purified the antigen recognized by B6H12 to homogeneity. Surprisingly, it is a 50-kD molecu1e that is expressed on the plasma membranes of all hematopoietic cells, including erythrocytes, which express no known integrins. On platelets and placenta, but not on erythrocytes, this protein is associated with an integrin that can be recognized by an anti-β3 antibody. In addition, both the anti-β3 and several mAbs recognizing the 50-kD protein inhibit Arg-Gly-Asp stimulation of phagocytosis. These data demonstrate an association between integrins and the 50-kD protein on several cell types. For this reason, we call it Integrin-associated Protein (IAP). We hypothesize that IAP may play a role in signal transduction for enhanced phagocytosis by Arg-Gly-Asp ligands.
AB - Phagocytosis by monocytes or neutrophils can be enhanced by interaction with several proteins or synthetic peptides containing the Arg-Gly-Asp sequence. Recently we showed that an mAb, B6H12, specifically inhibited this enhancement of neutrophi1 phagocytosis by inhibiting Arg-Gly-Asp binding to the leukocyte response integrin (Gresham, H.D., J.L. Goodwin, P.M. Allen, D.C. Anderson, and E.J. Brown. 1989. J. Cell Biol. 108:1935-1943). Now, we have purified the antigen recognized by B6H12 to homogeneity. Surprisingly, it is a 50-kD molecu1e that is expressed on the plasma membranes of all hematopoietic cells, including erythrocytes, which express no known integrins. On platelets and placenta, but not on erythrocytes, this protein is associated with an integrin that can be recognized by an anti-β3 antibody. In addition, both the anti-β3 and several mAbs recognizing the 50-kD protein inhibit Arg-Gly-Asp stimulation of phagocytosis. These data demonstrate an association between integrins and the 50-kD protein on several cell types. For this reason, we call it Integrin-associated Protein (IAP). We hypothesize that IAP may play a role in signal transduction for enhanced phagocytosis by Arg-Gly-Asp ligands.
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U2 - 10.1083/jcb.111.6.2785
DO - 10.1083/jcb.111.6.2785
M3 - Article
C2 - 2277087
AN - SCOPUS:0025666501
VL - 111
SP - 2785
EP - 2794
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 6 I
ER -