Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The location of peroxide-utilizing enzymes has been studied in rat brain. Glutathione peroxidase and glutathione reductase distributions indicate that both enzymes are located in the cytoplasm and in the matrix space of "synaptosomal" and "free" mitochondria. On the other hand, catalase distribution parallels that of NADH-cytochrome c reductase (rotenone-insensitive), and appears to be associated with the outer membrane of brain mitochondria. Whereas no gross age-dependent changes in various marker enzymes were found, a gradual but significant increase in glutathione peroxidase from the soluble fraction of free mitochondria was detected. The consequences of such increase are discussed with regard to the reducing potential of the cell.
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PMID:Age-dependent variations in peroxide-utilizing enzymes from rat brain mitochondria and cytoplasm. 622 5

Female F344 rats received an i.p. injection of iron-dextran (600 mg Fe/kg) and then after 1 week were fed a diet containing 0.02% hexachlorobenzene (HCB) for up to 65 weeks. All rats (8/8) which received HCB after iron overload developed multiple hepatic nodules whereas only 3/8 rats administered HCB alone had nodules (average of one per positive liver). These hyperplastic regions were depleted of iron and were often positive for gamma-glutamyl transpeptidase (GGT) and glutathione S-transferase P (GST-P). Telangiectasis and peliosis were prominent features in the lesions. Short-term experiments (5-15 weeks of iron/HCB treatments) showed that GGT and GST-P were induced early in the neoplastic process but not in discrete focal areas. Iron alone also caused some induction of these enzymes. Some cells with induced GST-P in either short or long term experiments also stained positively for this enzyme in the nucleus. Studies of cytochrome P450 mediated activities showed that at 5 and 15 weeks HCB had induced EROD (an estimate of CYP1A1), PROD (CYP2B1 activity) and BROD activities (CYP2B1 but also other isoenzymes). Under the influence of iron overload EROD was significantly depressed from HCB alone, but not the others or cytochrome P450 reductase. Cytosolic glutathione S-transferase activities were also induced by HCB, but, unlike microsomal EROD, preloading with iron enhanced the effects. In contrast, although cytosolic diaphorase activity was induced by HCB, this response was depressed in combination with iron. Glutathione peroxidase (with H2O2 as substrate) was depressed by both iron and HCB. Clearly, iron overload potentiates the neoplastic process induced by HCB in rats, with both enhancing and depressing effects on various enzyme activities induced by this chemical.
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PMID:Enhancement by iron of hepatic neoplasia in rats caused by hexachlorobenzene. 833 Mar 54

Liver and colon pro- and anti-oxidant enzyme activities were investigated in rats treated with ethylnitrosourea (ENU) (i.p.) (4 mg/kg body wt) for 6 months. The pro-oxidant enzymes (NADPH cytochrome c reductase, NADH cytochrome c reductase, NADH cytochrome b5 reductase and cytochrome P-4502E1and the antioxidant enzyme, superoxide dismutase (SOD) exhibited significantly increased activity in liver and colon. Glucose-6-phosphate dehydrogenase (G6PDH) and glutathione-S-transferase (GST) showed enhanced activity in liver, but decreased activity in colon. Glutathione peroxidase (GP) and glutathione reductase (GR) activities were significantly increased in colon, but decreased in liver. Catalase (CAT) activity while showed a significant increase in liver, exhibited only marginal increase in colon. Malondialdehyde (MDA) level was significantly elevated in both tissues.
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PMID:Liver and colon pro- and anti-oxidant enzyme activities in rats after long-term ethylnitrosourea exposure. 2290 Mar 2