title: Effect of zinc ions on fibrin network structure.
abstract: In addition to calcium, other physiologically important divalent cations (magnesium and zinc) are known to influence fibrin formation and structure. We have studied the effect of different concentrations (0-20 micromol/l) of zinc ions (Zn2+) in the absence and presence of calcium on the gel structure formed in purified fibrinogen-enzyme systems. For that purpose, we used turbidity measurement, liquid permeation and confocal three-dimensional microscopy of the gel as well as sodium dodecyl sulphate (SDS)-gel electrophoresis. The results of turbidity measurements indicated that the clotting time decreased with increasing concentrations of Zn2+. The fiber mass: length ratio (mu) values showed that the porosity of the gels increased in a concentration-dependent manner, i.e. at higher concentrations of Zn2+, larger pores with thicker fibrin fibers were formed. Three-dimensional microscopy data of the gels were in good agreement with the mu data. On SDS-gel electrophores of reduced fibrin, no cross-linking was observed in the presence of zinc ions only (without the addition of calcium ions), nor were D-D dimer bands observed in non-reduced plasmin digested fibrin samples in the presence of zinc ions only. The above results show that zinc changes the fibrin gel structure and that this effect appears to be independent of calcium.
authors.affiliation: Department of Laboratory Medicine/Coagulation Research, Karolinska Institute, Karolinska Hospital, Stockholm, Sweden. kafa@mb.ks.se
authors.forename: K
authors.initials: K
authors.lastname: Fatah
authors.forename: B
authors.initials: B
authors.lastname: Hessel
mesh_terms: D002118:Calcium / Q000737:chemistry / Q000494:pharmacology; D005337:Fibrin / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D018613:Microscopy, Confocal; D011487:Protein Conformation / Q000187:drug effects; D015032:Zinc / Q000737:chemistry* / Q000494:pharmacology
chemical_list: D005337:Fibrin; D015032:Zinc; D002118:Calcium