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Open AccessJournal ArticleDOI

Integrin-associated protein : a 50-kd plasma membrane antigen physically and functionally associated with integrins

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TLDR
The data demonstrate an association between integrins and the 50-kD protein on several cell types and hypothesize that IAP may play a role in signal transduction for enhanced phagocytosis by Arg-Gly-Asp ligands.
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-beta 3 antibody. In addition, both the anti-beta 3 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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Journal ArticleDOI

Cellular functions regulated by src family kinases

TL;DR: This chapter reviews the evidence implicating Src family kinases in specific receptor pathways and describes the mechanisms leading to their activation, the targets that interact with these kinases, and the biological events that they regulate.
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Signal transduction from the extracellular matrix.

TL;DR: There are many compelling examples of control of cell differentiation and gene expression through adhesive interactions with extracellular matrix, including activation of T-lymphocytes through the T-cell antigen receptor is markedly enhanced by integrin-mediated adhesion to fibronectin or laminin.
Journal ArticleDOI

Role of CD47 as a marker of self on red blood cells.

TL;DR: It is shown that CD47 (integrin-associated protein) functions as a marker of self on murine red blood cells and may represent a potential pathway for the control of hemolytic anemia.
References
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Journal ArticleDOI

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

TL;DR: A rapid and convenient method for peptide mapping of proteins has been developed that involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis.
Book ChapterDOI

Polyacrylamide Gel Electrophoresis of Viral Proteins

TL;DR: This chapter describes polyacrylamide gel electrophoresis of viral proteins in gels, which are extensively used at the present time and are more homogeneous and stable than other commonly used materials.
Journal ArticleDOI

Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression.

TL;DR: Investigating the effects of ligation of the fibronectin receptor (FnR) on gene expression in rabbit synovial fibroblasts demonstrated that signals leading to changes in gene expression are transduced by the FnR, a member of the integrin family of extracellular matrix receptors.
Journal ArticleDOI

Surface-specific iodination of membrane proteins of viruses and eucaryotic cells using 1,3,4,6-tetrachloro-3alpha,6alpha-diphenylglycoluril.

Markwell Ma, +1 more
- 31 Oct 1978 - 
TL;DR: The effectiveness, simplicity of use, and versatility of chloroglycoluril recommend it as an iodinating reagent for both surface-specific and nonvectorial labeling of membrane systems.
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