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Glutathione peroxidase glutathione reductase and glutathione transferase activities in the human artery vein and heart



Glutathione peroxidase glutathione reductase and glutathione transferase activities in the human artery vein and heart



Journal of Molecular & Cellular Cardiology 22(9): 935-938



The continuous exposure to blood components, including prooxidants, makes the blood vessel wall susceptible to oxidative stress and free radical mediated reactions (Henning and Chow, 1988; Stamm et al., 1989; Halliwell and Gutteridge, 1984). Free radicals can be produced extracellularly via the respiratory bursts of activated neutrophils, or intracellularly, via oxidation of hypoxanthine by xanthine oxidase (Henning and Chow, 1988; Stamm et al., 1989; Rubanyi, 1988). Microsomial enzymes such as lipoxygenase and cyclooxygenase may also be a source of reactive species of oxygen (Henning and Chow, 1988; Stamm et al., 1989; Rubanyi, 1988; Mason et al., 1980). It has been proposed that free radicals are involved in the initiation and progression of various cardiovascular diseases including arteriosclerosis (Henning and Chow, 1988; Stamm et al., 1989; Yagi, 1988; Jurgens et al., 1987). Thus the adequacy of the defence systems against free radicals is critical for the susceptibility of blood vessel wall to oxidative damage. Among the enzymatic systems capable of protecting the cell against oxidative injury, selenium dependent glutathione peroxidase (Se-GSH-px), glutathione reductase (GSSG-rx) and glutathione transferase (GST) play a crucial role (Flohe' et al., 1976; Mannervik and Danielson, 1988). Using glutathione (GSH) as cofactor, Se-GSH-px reduces H2O2 to water and organic hydroperoxides to the corresponding alcohols (Flohe' et al., 1976). This reaction leads to conversion of GSH into its oxidized form (GSSG). In the presence of NADPH, GSSG-rx is able to reduce the oxidized glutathione. GST consists of a family of enzymes that contributes to the cellular detoxification by catalyzing the GSH conjugation to electrophilic substrates, including carbonyl compounds like 4-hydroxyalkenals, which are toxic products of lipid peroxidation (Mannervik and Danielson, 1988; Danielson et al., 1987). Since there is not much information about the mechanisms devoted to protect the human blood vessels against free radical aggression, we have characterized the Se-GSH-px, GSSG-rx and the GST activities of the internal mammary artery and saphenous vein obtained from patients undergoing coronary revascularization. For comparison, we also studied the activities of the GSH-dependent enzymes of the human heart. Our data show that significantly different levels of Se-GSH-px, GSSG-rx and GST are present in the human artery, vein and heart thus suggesting a different antioxidative capacity of the three tissues to counteract the oxidative stress.

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Accession: 007380727

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PMID: 2280414

DOI: 10.1016/0022-2828(90)91033-4


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