Ukr.Biochem.J. 2014; Volume 86, Issue 5, Sep-Oct, pp. 82-88

doi: https://doi.org/10.15407/ubj86.05.082

Study of the sites of plasminogen molecule which are responsible for inhibitory effect of Lys-plasminogen on platelet aggregation

26.06.2015   Uncategorized   No comments

Y. M. Roka-Moya, D. D. Zhernossekov, E. I. Yusova,
L. G. Kapustianenko, T. V. Grinenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: chemikdd@mail.ru

Plasminogen/plasmin system is involved in such important processes as thrombosis, inflammation and cancer. Plasmin and plasminogen mediate their action through plasminogen-binding proteins on the cell surface. Lys-plasminogen, but not Glu-plasminogen, shows inhibitory effect on platelet aggregation induced by ADP, collagen and thrombin in preparations of both: platelet-rich plasma and washed platelets. We have shown that the kringle domains of Lys-plasminogen mediate interaction of this proenzyme with platelet-surface proteins. The aim of the work is to study the role of certain kringle domains in the inhibitory effect of Lys-plasminogen and to determine possible plasminogen-binding proteins on the platelet surface. All studied plasminogen fragments (K1-3, K4 and K5) abolished the inhibitory effect of Lys-plasminogen on platelet aggregation. We observed that K5 was more effective than K1-3 and K4. Biotin-labeled Lys-plasminogen, Glu-plasminogen and plasminogen fragment K1-3 possessed the highest affinity for actin, whereas the binding of biotin-labeled mini-plasminogen and K4 to actin was negligible. We have suggested that inhibitory effect of Lys-plasminogen is due to the interaction of kringle domains of this proenzyme with membrane-bound proteins which are exposed on the platelet surface during activation and are involved in thrombus formation.

Keywords: , , , ,

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