Please use this identifier to cite or link to this item: https://rep.polessu.by/handle/123456789/16964
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dc.contributor.authorRoka-Moya, Y.M.-
dc.contributor.authorZhernossekov, D.D.-
dc.contributor.authorYusova, E.I.-
dc.contributor.authorKapustianenko, L.G.-
dc.contributor.authorGrinenko, T.V.-
dc.date.accessioned2020-01-16T11:41:43Z-
dc.date.available2020-01-16T11:41:43Z-
dc.date.issued2014-
dc.identifier.citationStudy of the sites of plasminogen molecule which are responsible for inhibitory effect of Lys-plasminogen on platelet aggregation / Y.M. Roka-Moya [и др.] // Ukrainian Biochemical Journal. – 2014. – Vol. 86, № 5. – P. 82-88.ru
dc.identifier.urihttps://rep.polessu.by/handle/123456789/16964-
dc.description.abstractPlasminogen/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.ru
dc.language.isoen-
dc.rightsоткрытый доступru
dc.subjectplasminogen kringlesru
dc.subjectplatelet aggregationru
dc.subjectplatelet plasminogen receptorsru
dc.subjectLys-plasminogenru
dc.subjectactinru
dc.titleStudy of the sites of plasminogen molecule which are responsible for inhibitory effect of Lys-plasminogen on platelet aggregationru
dc.typeArticleen
Appears in Collections:Публикации сотрудников / Publications of the teaching stuff of Polessky State University



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