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

David A. Cheresh, Shlomo A. Berliner, Vicente Vicente, Zaverio M. Ruggeri

Research output: Contribution to journalArticlepeer-review

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 α chain (α residues 572-574) but fail to recognize the Arg-Gly-Asp sequence in the N-terminal region of the same chain (α 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 α 572-574 sequence, a site at the C-terminus of the γ chain (γ 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.

Original languageEnglish
Pages (from-to)945-953
Number of pages9
JournalCell
Volume58
Issue number5
DOIs
StatePublished - 8 Sep 1989
Externally publishedYes

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