IQUIBA-NEA   25617
INSTITUTO DE QUIMICA BASICA Y APLICADA DEL NORDESTE ARGENTINO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Contribution of the proteases in the hemostatic alterations induced by Bothrops alternatus venom.
Autor/es:
GAY, CLAUDIA C.; VAN DE VELDE, ANDREA C; LEIVA, LAURA C; BUSTILLO, S
Lugar:
Ciudad Autónoma de Buenos Aires
Reunión:
Congreso; XVIII Jornadas de la Sociedad Argentina de Biología; 2016
Institución organizadora:
Sociedad Argentina de Biología
Resumen:
Bothrops alternatus is a medical important snake in central and northern Argentina. Bothropic envenoming causes proteolysis of tissues, bleeding and coagulation disorders. Coagulating enzymes belong to two proteases families: snake venom serineproteinases (SVSPs) with thrombin-like activity and metalloproteinases (SVMPs) mainly as prothrombin activators; these latest representing more of 50% of B. alternatus venom components. In this work, contribution of metalloproteases in coagulation disorders was studied. The whole venom (10 mg/mL) was incubated with an inhibitor of SVMPs, EDTA-Na2 (10 mM), the excess of inhibitor was previously removed by passing the mixture by Sephadex G-25 (venom without inhibitor was subjected to the same process). Clotting time (CT) was recorder using citrated plasma or fibrinogen (3.5 mg/mL) incubated with venom or venom-EDTA-Na2 (venom final concentration was 270 µg/mL). Results showed that venom-EDTA-Na2 was able to cause a delay of 3.5 times of the CT on citrated plasma compared with venom alone. However, venom-EDTA-Na2 did not alter fibrinogen CT. Results suggest presence of both proteases families in the venom of B. alternatus: metalloproteases acting mainly as pro-coagulant factors. Because of SVMPs are the most important components of this venom, they become relevant targets for the development of new therapeutic agents.