title: Low-affinity interaction of fibrinogen carboxy-gamma terminus with human monocytes induces an oxidative burst and modulates effector functions.
abstract: The interaction of highly purified, monomeric fibrinogen (Fg) with human monocytes (MO) was investigated. In contrast to commercial Fg, no high-affinity binding of monomeric Fg to MO or mononuclear cells could be demonstrated. MO preincubated with Fg in the presence or absence of Ca++ elicited an oxidative burst when triggered with anti-Fg antibodies. Divalency of the antibody and specificity were required, but an intact Fc portion was not. Surface-adsorbed monomeric Fg also promoted an oxidative burst. Evidence is presented that Fg-MO interaction is mediated by the carboxy-gamma terminus of Fg. MO treated with monomeric Fg or exposed to Fg-coated surfaces show a reduced oxidative burst upon triggering with unrelated stimuli. Thus, MO function may be modulated upon interaction with surface-adsorbed Fg or with fibrin.
authors.affiliation: Institute of Veterinary Virology, University of Berne, Switzerland.
authors.forename: C
authors.initials: C
authors.lastname: Trezzini
authors.forename: T W
authors.initials: TW
authors.lastname: Jungi
authors.forename: F E
authors.initials: FE
authors.lastname: Maly
authors.forename: M
authors.initials: M
authors.lastname: Vittoz
authors.forename: E
authors.initials: E
authors.lastname: Peterhans
mesh_terms: D005340:Fibrinogen / Q000302:isolation & purification / Q000502:physiology*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008163:Luminescent Measurements; D009000:Monocytes / Q000378:metabolism*; D010101:Oxygen Consumption; D010446:Peptide Fragments / Q000378:metabolism; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism; D013481:Superoxides / Q000097:blood*
chemical_list: D010446:Peptide Fragments; D010980:Platelet Membrane Glycoproteins; D013481:Superoxides; D005340:Fibrinogen