ROLDAN OLARTE Eugenia Mariela
congresos y reuniones científicas
Identification of plasminogen activators in hamster oviduct
JIMÉNEZ DÍAZ, M; MARIELA ROLDÁN OLARTE; PEREYRA-ALFONSO, S; SANCHEZ, V.; FLORES, V
Tafi del Valle, Tucuman, Argentina
Jornada; XV Jornadas Científicas de la Sociedad de Biología de Tucumán; 1998
Sociedad de Biología de Tucumán
Proteolytic enzymes that participate in fertilization have not positively identified. We have characterized a serine protease homornally regulated in the hamster oviduct that might play a role in the activation of plasminogen (Plg) / plasmin (P) system in the extracellular matrix (ECM) of the eggs. Plg is significantly higher in the ovaric oocytes zona pellucida and over oviductal eggs plasmatic membranes .The aim of this work was to demonstrate that oviducal protease could be plasminogen activator (tPA). Determination of PA activities were performed in Tritón X- 100 treated tissue crude membrane fraction (E 1) and oviducal secretion of superovulated females. In the oviducal fluid just a litlle percentage of their proteolytic activity is plasminogen dependent probably due to the inactivation of PA (half life in plasma is 5 min). In El oviducal fraction the 100% of the activity is plasminogen dependent. The use of a selective uPA inhibitor (Amiloride) show that 90 % of activity is due tot-PA and 10 % to uPA whereas in uterus all activity is tPA. The specific aclivity were 1220 mIU/mg in oviduct and 2320 mIU/mg in uterus. Streptokinase (SK), a non enzimatic protein forms with the Plg a complex that has PA activity and awas used for studying the effect of plasminogen activation. The effect fo the SKproduces a change in the physico-chemical properties of the pellucida zone that could be involved in fertilization and development mechanism.