Human fibroblast adhesion to fibrinogen

David H. Farrell, Hamid A. Al-Mondhiry

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Fibrinogen and fibrin mediate the adhesion of many cell types. In this report, the adhesion sites for human dermal fibroblasts on fibrinogen are identified and characterized. Fibroblasts showed a time- and dose-dependent adhesion to fibrinogen. Using a combination of synthetic peptide mimetics, monoclonal antibodies, and recombinant fibrinogens, two major classes of adhesive sites were identified. One class was RGD-dependent and involved the RGD sites in the α chain of fibrinogen. α(v) integrins present on fibroblasts appeared to mediate this adhesion. Inhibition studies showed that the RGD-independent site was blocked by an ICAM-1 antagonist peptide. Furthermore, the inhibition was additive with RGD peptide inhibition and accounted for essentially all of the fibroblast adhesion. Together, these results suggest that fibroblast adhesion to fibrinogen is mediated by both α(v) integrins and ICAM-1.

Original languageEnglish (US)
Pages (from-to)1123-1128
Number of pages6
JournalBiochemistry
Volume36
Issue number5
DOIs
StatePublished - Feb 4 1997

ASJC Scopus subject areas

  • Biochemistry

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