Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Many anticancer drugs exert their cytotoxic effects via formation of oxygen free radicals. Cellular thiols, glutathione (GSH)-dependent enzymes and other redox enzymes are involved in the metabolism of these anticancer drugs and of the oxygen free radicals that may be generated during their metabolism. We quantified these biochemical parameters in cytosol from human ovarian tissues. We compared non-protein thiol levels, GSH transferase, GSH peroxidase, superoxide dismutase, catalase, DT diaphorase and aldehyde dehydrogenase activity in serous ovarian tumors (n = 15), other malignant ovarian tumors (n = 12), benign ovarian tissue (n = 10) and histologically normal ovarian tissue (n = 12). Mean GSH transferase and DT diaphorase activities were similar in serous and other malignant ovarian tumors. GSH transferase activity was decreased in malignant tissues relative to normal and benign tissues. Mean DT diaphorase and superoxide dismutase activities were increased in the malignant tissues, although this was not statistically significant. The mean levels of all enzymes except superoxide dismutase and aldehyde dehydrogenase in benign tissues were fairly similar to the mean levels found in normal tissue samples. Tissues from patients with serous ovarian tumors, who had received cyclophosphamide and cisplatin prior to surgery, also were analyzed (n = 7). Except for aldehyde dehydrogenase, all the parameters measured were decreased in these samples relative to serous tissue from untreated patients. These biochemical analyses may be useful in understanding the mechanisms involved in the response to chemotherapy.
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PMID:Detoxifying enzymes in human ovarian tissues: comparison of normal and tumor tissues and effects of chemotherapy. 239 58

F344 Male rats weighting between 90 and 110 gm were given 90 ppm diethylnitrosamine in their drinking water for 5 weeks. Seven weeks after the administration of carcinogen was completed, the rats were sacrificed and sections of their livers were embedded in methacrylate. Serial sections 2 or 4 micron in thickness demonstrated the presence of gamma-glutamyl transpeptidase, acid phosphatase, adenosine triphosphatase, aldehyde dehydrogenase, alkaline phosphatase, alpha-naphthyl butyrate esterase, DT diaphorase, glucose-6-phosphate dehydrogenase, and 5'-nucleotidase activity and glycogen. The use of 4-micron sections of methacrylate-embedded tissue allows the evaluation of many more phenotypic markers in serial sections than is currently possible with frozen sections.
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PMID:Examination of enzyme-altered foci with gamma-glutamyl transpeptidase, aldehyde dehydrogenase, glucose-6-phosphate dehydrogenase, and other markers in methacrylate-embedded liver. 287 68

Enzyme histochemistry performed on the liver of pregnant and non pregnant rats indicates that methadone (ME) does not cause direct damage to the cells. On the other hand, the enzyme aldehyde dehydrogenase was decreased in the periportal tract of the liver lobule of pregnant rats treated with 10 mg/kg ME for 20 days. NADPH dehydrogenase was increased in the central areas of the liver lobule within 3 days of ME treatment. It is suggested that a derangement of xenobiotic metabolizing enzymes in the liver, as well as in other organs, may be contribute to some of the alterations observed in ME treated animals.
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PMID:Methadone affects the histochemical pattern of xenobiotic-metabolizing enzymes in the liver of pregnant rats. 659 89

Serotonin-, dopamine-, and noradrenergic nuclei in human brainstem were examined histochemically for alcohol dehydrogenase, aldehyde dehydrogenase, and NADPH diaphorase. The findings indicate that monoaminergic centers are characterized by different repertoire of NO-ergic and ethanol-oxidizing enzymes, whose distribution correlates with the transmitter specialization of neurons.
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PMID:Ethanol-oxidizing and NO-synthesizing enzymes in monoaminergic nuclei of human brain. 1463 11