ANTIPLATELET ACTIVITY OF StSBTc-3, A SUBTILISIN-LIKE SERINE PROTEASE OF Solanum tuberosum

GUSTAVO R. DALEO,; PEPE, A.; MARÍA G. GUEVARA.; WHITEHEART, SYDNEY W,

Capital Federal

Congreso; Reunión Conjunta de Sociedades de Biociencias; 2017

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB)

Cardiovascular disease is one of the leading death causes worldwide. Antiplatelet and anticoagulant therapies improved in the last decades but the search of new therapeutic possibilities it´s still a necessity. The aim of the present work is to characterize the antiplatelet activity of a subtilisin-like protease of potato (StSBTc-3).Washed platelets in HEPES Tyrode buffer with human fibrinogen and CaCl2 were incubated with thrombin and the percentage of clot size relative to initial suspension volume was determined. StSBTc-3 inhibits clot retraction. We observed complete lack of clot retraction at all times assayed. Fibrinogen was added exogenous and is not limiting.To further investigate the possible action mechanism, platelet aggregation was measured using three different agonists (A23187, convulxin and thrombin) at different concentrations. All the experiments were repeated three times. StSBTc-3 inhibits platelet aggregation induced by all agonists tested. These result suggest StSBTc-3 blocks different pathways of the aggregation process. StSBTc-3 has potent antiplatelet activity and it´s a interesting protease to be evaluated for antiplatelet therapy. We´ll perform other analysis to further characterize the therapeutic potential of this enzyme.