Research PapersMore porous fibrin gel structure obtained by interaction with Lys-plasminogen than with Glu-plasminogenFatah-Ardalani, K.; Wallén, P.; Petersen, L. C.; Blombäck, M.Author Information P. Wallén and M. Blombäck are with the Department of Laboratory Medicine/Coagulation Research, Karolinska Institutet, Karolinska Hospital, Stockholm, Sweden, and L. C. Petersen is with Novo Nordisk A/S, Tissue Factor/Factor VII Research, Maaloev, Denmark. P. Wallén, deceased January 1999. K. Fatah-Ardalani is currently working at Pharmacia & Upjohn, Stockholm but the work was carried out at Karolinska Institute. Received 9 July 1999; revised 31 January 2000; accepted 7 February 2000 Sponsorship: This study was supported by grants from Gustaf the Vth 80 years fund, Torsten and Ragnar Söderberg foundation (1998), and the Swedish Match. K. Fatah-Ardalani Address correspondence to: Margareta Blombäck, Coagulation Research, Clinical Chemistry Building L2, 5th floor, Karolinska Hospital, 171 76 Stockholm, Sweden. Tel: (+46) 8 5177 4437; fax: (+46) 8 312 438; e-mail: [email protected] Blood Coagulation and Fibrinolysis: June 2000 - Volume 11 - Issue 4 - p 335-342 Buy Abstract 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 μ 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 ε-aminocaproic acid. The same results were obtained in plasma milieu for both μ andKs 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. © 2000 Lippincott Williams & Wilkins, Inc.