Journal archive > 2004 > N5, September-October

The ?-2-antiplasmin binding with fibrinogen/fibrin and their fragments independent of factor XIII

M. B. Zadorozhna, T. V. Grinenko, O. I. Yusova, G. L. Volkov

Possible interaction of ?-2-antiplasmin with fibrinogen, fibrin and their fragments independent of factor XIII as well as the inhibitor effect on the Glu-plasminogen activation by tissue activator were studied. It was shown that ?-2-antiplasmin is adsorbed on desAA- and desAABBfibrin films (K69.0 ± 1.0 nМ 68.6 ± 5.3 nМ, respectively). Glu-Plasminogen has no effect on the inhibitor binding with desAABBfibrin. ?-2-Antiplasmin shows strong affinity for fibrin D-dimer (Kd 65.0 ± 4.0 nМ) and D-fragment of fibrinogen (Kd 119.0 ± 21.0 nМ), but it does not interact with E-fragment. The inhibitor inside the fibrin clot decreases 10 times the activation rate of Glu-plasminogen by the tissue activator both is the presence and without factor XIII at physiological ratio of Glu-plasminogen, tissue activator, fibrin and ?-2-antiplasmin.

Thus we have shown that fibrinogen/fibrin binds ?-2-antiplasmin independent of the factor XIII. Binding sites of the inhibitor are localized in D-fragment of fibrinogen and/or fibrin D-dimer. ?-2-Antiplasmin inhibits the Glu-plasminogen activation by tissue activator on fibrin.


Recieved: 2004-03-05

Published at the site: 2004-10-10