Zinc inhibits FPA release and increases fibrin turbidity
- 1 August 1986
- journal article
- research article
- Published by Wiley in American Journal of Hematology
- Vol. 22 (4) , 347-353
- https://doi.org/10.1002/ajh.2830220403
Abstract
Physiologic concentrations of Zn(II) (4–40 μM) can increase the rate of thrombin‐induced fibrin clot formation (decreased clotting time, CT) and increase the turbidity of the fibrin gel. Both the initial and ultimate turbidity (Abs600 mm) of fibrin gels are increased in the presence of Zn(II). Two techniques were used to elaborate the mechanisms of Zn+2 procoagulant effect. Analytical ultracentrifugation indicates that Zn(II) does not induce the formation of fibrinogen multimers. Radioimmunoassay for FPA indicates that thrombin activation of fibrinogen is decreased by Zn(II), with 50% inhibition of FPA release observed at 35 μM Zn(II). These experiments indicate that the critical feature of Zn(II) procoagulant effect is not due to the induction of fibrinogen proteolysis by thrombin, which is actually decreased. Rather, it appears that Zn(II) accelerates the polymerization step of fibrin assembly and concomitantly modifies fibrin gel structure.Keywords
This publication has 25 references indexed in Scilit:
- The procoagulant effect of zinc on fibrin clot formationAmerican Journal of Hematology, 1985
- Interaction of fibrinogen with mercuryThrombosis Research, 1983
- FACTORS INFLUENCING FIBRIN GEL STRUCTURE STUDIED BY FLOW MEASUREMENT*Annals of the New York Academy of Sciences, 1983
- FIBRINOPEPTIDE B IN FIBRIN ASSEMBLY AND METABOLISM: PHYSIOLOGIC SIGNIFICANCE IN DELAYED RELEASE OF THE PEPTIDE*Annals of the New York Academy of Sciences, 1983
- FIBRIN ASSEMBLY*Annals of the New York Academy of Sciences, 1983
- CALCIUM ION FUNCTIONS IN FIBRINOGEN CONVERSION TO FIBRINAnnals of the New York Academy of Sciences, 1983
- CALCIUM‐BINDING REGIONS IN FIBRINOGEN*Annals of the New York Academy of Sciences, 1983
- Effects of divalent cations on the conversion of fibrinogen to fibrin and fibrin polymerizationAmerican Journal of Hematology, 1982
- Structural features of fibrinogen associated with binding to chelated zincBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1981
- A two-step fibrinogen–fibrin transition in blood coagulationNature, 1978