title: Human fibroblast adhesion to fibrinogen.
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 alpha chain of fibrinogen. alpha 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 alpha V integrins and ICAM-1.
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, College of Medicine, Hershey 17033, USA. dfarrell@bcmic.hmc.psu.edu
authors.forename: D H
authors.initials: DH
authors.lastname: Farrell
authors.forename: H A
authors.initials: HA
authors.lastname: al-Mondhiry
mesh_terms: D000595:Amino Acid Sequence; D002448:Cell Adhesion / Q000187:drug effects; D002478:Cells, Cultured; D005340:Fibrinogen; D005347:Fibroblasts / Q000166:cytology / Q000502:physiology; D006801:Humans; D007231:Infant, Newborn; D007700:Kinetics; D008297:Male; D009842:Oligopeptides / Q000494:pharmacology*; D011994:Recombinant Proteins; D012867:Skin / Q000166:cytology; D012879:Skin Physiological Phenomena
chemical_list: D009842:Oligopeptides; D011994:Recombinant Proteins; C047981:arginyl-glycyl-aspartic acid; D005340:Fibrinogen; C058161:glycyl-arginyl-glycyl-aspartyl-seryl-proline; C058347:glycyl-arginyl-glycyl-glutamyl-seryl-proline