Abstract
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 neutrophil 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 molecule 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2785-2794 |
| Number of pages | 10 |
| Journal | Journal of Cell Biology |
| Volume | 111 |
| Issue number | 6 PART 1 |
| State | Published - Dec 1990 |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
Cite this
Integrin-associated protein : A 50-kD plasma membrane antigen physically and functionally associated with integrins. / Brown, Eric; Hooper, Lora; Ho, Thang; Gresham, Hattie.
In: Journal of Cell Biology, Vol. 111, No. 6 PART 1, 12.1990, p. 2785-2794.Research output: Contribution to journal › Article
}
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
PY - 1990/12
Y1 - 1990/12
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 neutrophil 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 molecule 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 neutrophil 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 molecule 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.
UR - http://www.scopus.com/inward/record.url?scp=0025666501&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025666501&partnerID=8YFLogxK
M3 - Article
VL - 111
SP - 2785
EP - 2794
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 6 PART 1
ER -