Complexation with heparin prevents adhesion between fibrin-coated surfaces.

G.S Retzinger,L.J Chandler,B.C Cook

doi:10.1016/s0021-9258(18)35773-9

G.S Retzinger, L.J Chandler + Show 1 more

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https://doi.org/10.1016/s0021-9258(18)35773-9

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Abstract

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.

Highlights

- Heparin, inLangmuirianfashion, binds stoichiometrically withhigh affinity, Kd 100 nM, to both fibrinogen and fibrin adsorbed as monomolecular films to lecithin-coated, microscopic, polystyrene-divinylbenzene beads
On the bead system is anideal tool with which to probe the interacbasis of this observation, it has been assumed that the mecht-ions of heparin with adsorbed fibrin(ogen) because: 1) the anism by which endogenous heparin inhibits coagulation is only fibrin(ogen)isthatspreadas amonolayer on beads, solely derived from its interaction with these plasma factors which can be readily separated from the solution by centrif
Rate of Dissociation of Aggregates of Fibrin-coated Beads as a Measure of Heparin Concentration-Both thrombinand atroxin catalyze fibrin formation, the former liberating both fibrinopeptide A (FpA) and FpB, the latter liberating only beads coated with a mixed film of lecithin and fibrin(ogenw) ere used FpA (35)

Summary

Introduction

- Heparin, inLangmuirianfashion, binds stoichiometrically withhigh affinity, Kd 100 nM, to both fibrinogen and fibrin adsorbed as monomolecular films to lecithin-coated, microscopic, polystyrene-divinylbenzene beads. - The ability to dissociate aggregates of fibrin-coated beads is not unique to porcine heparin of Mrcave, 14,250 that was used to generate the data of Fig. 3.

Results

Conclusion