More porous fibrin gel structure obtained by interaction with Lys-plasminogen than with Glu-plasminogen.
The effect of Glu1- and Lys78-plasminogen on the assembly and structure of fibrin gels was studied in purified fibrinogen-thrombin system and in plasminogen-free plasma, using turbidity, liquid permeation and three-dimensional (3D) confocal laser microscopy methods. In the purified fibrinogen system using the turbidity method, the final optical density of the fibrin gels increased with increasing concentrations of Lys-plasminogen. The fiber mass/length ratio mu increased with increasing concentrations of both Glu1- and Lys78-plasminogen, the effect of Lys78-plasminogen being much stronger. The permeability coefficient (Ks) analyzed with the permeation method revealed that fibrin gels formed in the presence of Lys78-plasminogen were more permeable (porous) than the control gels. The effect on the gel structure was inhibited by the fibrinolytic inhibitor epsilon-aminocaproic acid. The same results were obtained in plasma milieu for both mu and Ks as in the purified system, i.e. the gels became more porous with increasing concentrations of Lys78-plasminogen. 3D microscopy pictures of the gels verified the findings.
Fatah-Ardalani
K
K
Department of Laboratory Medicine/Coagulation Research, Karolinska Institutet, Karolinska Hospital, Stockholm, Sweden.
Wallén
P
P
Petersen
L C
LC
Blombäck
M
M
D001777:Blood Coagulation; D005337:Fibrin / Q000737:chemistry*; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D010958:Plasminogen / Q000737:chemistry*; D013499:Surface Properties
D010446:Peptide Fragments; C018998:lysyl-plasminogen; D005337:Fibrin; D010958:Plasminogen