Complexation with heparin prevents adhesion between fibrin-coated surfaces

• Published in: The Journal of biological chemistry Vol. 267; no. 34; pp. 24356 - 24362
• Main Authors: RETZINGER, G. S, CHANDLER, L. J, COOK, B. C
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 05-12-1992
• Subjects: Adsorption; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Carbohydrates; Crotalid Venoms - metabolism; Dextran Sulfate - pharmacology; Fibrin - metabolism; Fibrinogen - metabolism; Fundamental and applied biological sciences. Psychology; Heparin - metabolism; Heparin - pharmacology; Heterosides; Humans; Kinetics; Nephelometry and Turbidimetry; Other biological molecules; Peptide Fragments - isolation & purification; Phosphatidylcholines - metabolism; Polystyrenes; Resins, Synthetic; Swine; Fibrin; Regulation(control); Coated particle; Molecular interaction; Carbohydrate; Heparin; Adhesion; Quantitative analysis
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)35773-9

Heparin, in Langmuirian fashion, binds stoichiometrically with high affinity, Kd approximately 100 nM, to both fibrinogen
and fibrin adsorbed as monomolecular films to lecithin-coated, microscopic, polystyrene-divinylbenzene beads. Complex formation
inhibits aggregation of fibrin-coated beads, and it also results in dissociation of preformed aggregates of fibrin-coated
beads. These phenomena are not caused by desorption of fibrin(ogen), indirect inhibition of thrombin activity, or mere electrostatic
repulsion of charged particles. Instead, these data are consistent with the proposal that the complexed heparin interferes
directly with dimer formation between fibrin molecules adsorbed to colliding beads. We describe these phenomena and their
application to the development of sensitive analytical methods for quantitating heparin. Based on these observations, we also
propose a role for endogenous heparin in the physiologic regulation of fibrin-mediated adhesion of surfaces.