Glutathione peroxidase (GSH-Px), together with catalase, superoxide dismutase and vitamin E, is involved in the antioxidant defense of living organisms. It reduces toxic lipid hydroperoxides to harmless hydroxides, utilizing GSH as a reducing agent. Selenium (Se)-dependent GSH-Px contains Se as a prosthetic group, and its activity is related to the levels of the element in diet. In the present research we investigated the influence of Se administration on PGI2 production. Se was added to drinking water for 80 days (1 mg/l sodium selenite corresponding to a daily intake of 0.3 ppm/rat). At the end of the period, the aorta, cava vein, lower lung lobe and heart apex were removed and specimens were incubated in 0.15 M Tris-HCl pH 9.37 to assess PGI2-like activity (PGI2-LA) (aggregometric method). GSH-Px activity was measured in erythrocytes to verify the effectiveness of Se treatment. We observed a 90% increase of GSH-Px activity (p < 0.005, n = 8) in Se-supplemented rats. Aorta synthesized more PGI2-LA production in the aorta (+44%; p < 0.005, n = 12) but not in the cava vein, lung or heart. The incubation of aortas from Se-treated rats with 0.2 M 3-amino-1,2,4-triazole, a GSH-Px inhibitor, resulted in a 90% reduction (p < 0.02, n = 5) of PGI2-LA synthesis. Present results indicate that GSH-Px plays a role in PGI2-LA production in arterial walls, suggesting that a decrease in the level of peroxides, in conditions of high GSH-Px activity, may increase PGI2-LA generation.