Intravenous apyrase administration reduces arterial thrombosis in a rabbit model of endothelial denudation in vivo

Costa, AF; Gamermann, PW; Picon, PX; Mosmann, MP; Kettlun, AM; Valenzuela, MA.; Sarkis, JJF; Battastini, AMO; Picon, PD

Abstract

The role of adenine nucleotides on vascular and platelet functions has long been established. Apyrass (CD39) takes part of a family of ecto-enzymes that hydrolyse adenosine diphosphate and adenosine triphosphate. The participation of apyrase in the thromboregulatory system is under study. An in vivo experimental model of acute arterial thrombosis was used to test the hypothesis that administering a soluble form of potato apyrase could prevent thrombus formation. Twenty-five white New Zealand male rabbits suffered balloon aortic endothelium denudation and, after 15 days, they were submitted to a thrombosis-triggering protocol with a procoagulant (Russel's viper venom) and epinephrine. After the thrombosis-triggering protocol, 12 animals received two soluble apyrase administrations intravenously (with 90 min intervals), while 13 control animals received no apyrase. Three hours after the triggering protocol, the animals were killed and the rate and area of arterial thrombosis were analyzed. The rate of thrombosis in the apyrase group was significantly lower than that of the control group (16.7 versus 69%, respectively; P = 0.015), as was the area of thrombosis (1.7 ± 4.3 versus 21.7 ± 37.4 mm2, respectively; P = 0.008). Our results confirm that apyrase participates in homeostasis through a potent antithrombotic effect. © 2004 Lippincott Williams & Wilkins.

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Título según WOS: Intravenous apyrase administration reduces arterial thrombosis in a rabbit model of endothelial denudation in vivo
Título según SCOPUS: Intravenous apyrase administration reduces arterial thrombosis in a rabbit model of endothelial denudation in vivo
Título de la Revista: BLOOD COAGULATION & FIBRINOLYSIS
Volumen: 15
Número: 7
Editorial: LIPPINCOTT WILLIAMS & WILKINS
Fecha de publicación: 2004
Página de inicio: 545
Página final: 551
Idioma: English
Notas: ISI, SCOPUS