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Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells

Academic Article
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Overview

authors

  • Cheresh, D. A.
  • Berliner, S. A.
  • Vicente, V.
  • Ruggeri, Zaverio

publication date

  • September 1989

journal

  • Cell  Journal

abstract

  • Endothelial cells and activated platelets express integrin-type receptors responsible for adhesion to fibrinogen. We have located distinct integrin-directed endothelial cell and platelet attachment sites on immobilized fibrinogen using a combination of synthetic peptides, fibrinogen fragments, and specific anti-peptide monoclonal antibodies. Endothelial cells exclusively recognize an Arg-Gly-Asp-containing site near the C-terminus of the alpha chain (alpha residues 572-574) but fail to recognize the Arg-Gly-Asp sequence in the N-terminal region of the same chain (alpha residues 95-97). In contrast, platelets do not require either Arg-Gly-Asp sequence for binding to intact fibrinogen and are capable of recognizing, in addition to the alpha 572-574 sequence, a site at the C-terminus of the gamma chain (gamma residues 400-411). These data suggest a molecular mechanism whereby platelets and endothelial cells interact with distinct sites on the fibrinogen molecule during hemostasis and wound healing.

subject areas

  • Antibodies, Monoclonal
  • Antigens, Surface
  • Binding Sites
  • Blood Platelets
  • Cell Adhesion
  • Cell Adhesion Molecules
  • Endothelium, Vascular
  • Fibrinogen
  • Humans
  • Immunologic Techniques
  • In Vitro Techniques
  • Platelet Membrane Glycoproteins
  • Structure-Activity Relationship
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(89)90946-x

PubMed ID

  • 2673537
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Additional Document Info

start page

  • 945

end page

  • 953

volume

  • 58

issue

  • 5

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