tailieunhanh - Báo cáo khoa học: Dual modulation of prothrombin activation by the cyclopentapeptide plactin

Plactin, a family of cyclopentapeptides, enhances fibrinolytic activity by elevating the activity of cellular urokinase-type plasminogen activator (u-PA), a protease involved in a variety of extracellular proteolytic events. Factor(s) in the blood plasma is an absolute requirement for this plactin activity. | Dual modulation of prothrombin activation by the cyclopentapeptide plactin Tomotaka Harada Tomoko Tsuruta Kumi Yamagata Toshiki Inoue and Keiji Hasumi Department of Applied BiologicalScience Tokyo Noko University Tokyo Japan Keywords blood coagulation fibrinolysis proteolysis prothrombin urokinase Correspondence K. Hasumi Department of Applied Biological Science Tokyo Noko University 3-5-8 Saiwaicho Fuchu-shi Tokyo 183 8509 Japan Fax 81 42 367 5708 Tel 81 42 367 5710 E-mail hasumi@ These authors contributed equally to this work Received 30 January 2009 revised 17 February 2009 accepted 20 February 2009 doi Plactin a family of cyclopentapeptides enhances fibrinolytic activity by elevating the activity of cellular urokinase-type plasminogen activator u-PA a protease involved in a variety of extracellular proteolytic events. Factor s in the blood plasma is an absolute requirement for this plactin activity. In this study we found that plactin promoted plasma cofactordependent conversion of inactive single-chain u-PA to active two-chain u-PA on U937 cells. Using plactin-affinity chromatography we identified prothrombin as one of the plasma cofactors. In incubations of U937 cells with prothrombin and Xa plactin increased the formation of thrombin which cleaved single-chain u-PA to afford the inactive two-chain form. Thrombin-cleaved two-chain u-PA was alternatively activated by cellular cystatin-sensitive peptidase activity yielding fully active two-chain u-PA. In a purified system plactin bound to prothrombin altered its conformation and dually modulated factor Xa-mediated proteolytic activation of prothrombin to a-thrombin. Plactin inhibited the activation catalyzed by Xa in complex with Va Ca2 and phospholipids prothrombinase whereas the activations catalyzed by nonmembrane-associated Xa were enhanced markedly by plactin. Plactin inhibited in vitro plasma coagulation which involved prothrombinase formation. Plactin did not

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