Integrin-associated protein

A 50-kD plasma membrane antigen physically and functionally associated with integrins

Eric Brown, Lora Hooper, Thang Ho, Hattie Gresham

Research output: Contribution to journalArticle

275 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)2785-2794
Number of pages10
JournalJournal of Cell Biology
Volume111
Issue number6 PART 1
StatePublished - Dec 1990

Fingerprint

Staphylococcal Protein A
Integrins
Cell Membrane
Phagocytosis
Antigens
Proteins
Neutrophils
Erythrocytes
Placenta
Monocytes
Anti-Idiotypic Antibodies
Signal Transduction
Blood Platelets
Ligands
Peptides

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 journalArticle

@article{7dddc122f8c1463c8d8a9eff997c8860,
title = "Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins",
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.",
author = "Eric Brown and Lora Hooper and Thang Ho and Hattie Gresham",
year = "1990",
month = "12",
language = "English (US)",
volume = "111",
pages = "2785--2794",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "6 PART 1",

}

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 -