Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.9.3.1 (cytochrome oxidase)
8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human blood mononuclear cells exposed to visible light increase their antioxidant enzyme (superoxide dismutase, catalase, and glutathione peroxidase) and DT-diaphorase activities. The activities of CuZn-superoxide dismutase (3.70 +/- 0.25 U/mg protein), catalase (4.60 +/- 0.39 U/mg protein), and DT-diaphorase (1.40 +/- 0.11 mumol DCPIP/min.mg protein) increased 1.5-fold when mononuclear cells were exposed at 38 W/m2 for 4 h. Se-containing glutathione peroxidase activity (6.76 +/- 0.21 mU/mg protein) increased 1.3 times after 3 h of exposure to 38 W/m2. Conversely, Mn-superoxide dismutase (2.20 +/- 0.20 U/mg protein), succinate dehydrogenase (0.86 +/- 0.04 mumol DCPIP/min.mg protein), and cytochrome oxidase (0.54 +/- 0.04 min-1 (k')/mg protein) activities remained constant during this period of exposure. The treatment of cells with cycloheximide prevented the response triggered by light exposure. These results introduce new insight to the adaptive response of human cells to light stress suggesting that: (a) the response observed might be ascribed to synthesis of stress proteins rather than to activation of a preexisting pool, and (b) that DT-diaphorase and CuZn-superoxide dismutase may operate biologically in a concerted fashion resulting in antioxidant activity.
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PMID:Induction of antioxidant enzymes and DT-diaphorase in human blood mononuclear cells by light stress. 837 61

The activity of some enzymes associated with peroxide metabolism and cytochrome oxidase activity was measured in cortex, striatum, hypothalamus, and hippocampus from brains of rats aged either 4, 15, or 27 months. Cytochrome oxidase activity was greatest in the cortex, but no significant age-related changes in the activity of cytochrome oxidase, superoxide dismutase, or glutathione peroxidase were found in any of the brain areas. In contrast, glutathione reductase activity increased as a function of age in all regions. In general, the activity of catalase fell on maturation of the animal to adulthood and then showed a trend to increase with age.
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PMID:The effect of age on the activity of enzymes of peroxide metabolism in rat brain. 838 67

The subcellular site of oxidation of [1-14C]phytanic acid to pristanic acid and CO2 was examined by measurement of the release of 14CO2 in different organelles from human and rat tissues prepared by isopycnic density gradient centrifugation in Nycodenz. The activity of phytanic acid oxidation in human tissues (liver and cultured skin fibroblasts) paralleled that of the peroxisomal marker catalase. We also observed that Nycodenz (commonly used gradient material for isolation of subcellular organelles) has a strong inhibitory effect on the alpha-oxidation of phytanic acid. This inhibition is reversible and can be decreased or eliminated by dialysis of isolated organelles against isotonic solution. The dialysis of endoplasmic reticulum, mitochondrial, and peroxisomal fractions from human liver and cultured skin fibroblasts for 2 h against isotonic solution increased the specific activity of phytanic acid oxidation by 1.3-, 1.3-, and 5-21-fold, respectively, after removal of Nycodenz as compared with nondialyzed samples. After dialysis, the rate of oxidation of phytanic acid in peroxisomes from human liver and cultured skin fibroblasts was 4-26 times higher than that in mitochondria and 43-130 times than that in the endoplasmic reticulum, suggesting that, in human tissues, phytanic acid is oxidized to pristanic acid in peroxisomes. On the other hand, the oxidation of phytanic acid in rat liver paralleled the distribution of the mitochondrial marker cytochrome-c oxidase. The 18-fold higher rate of oxidation in dialyzed mitochondria (198.6 +/- 4.20 pmol/h/mg of protein) than in peroxisomes (11.0 +/- 0.5 pmol/h/mg of protein) demonstrates that, in rodents, phytanic acid is oxidized in mitochondria. 2-[5-(4-Chlorophenyl)pentyl]oxiran-2-carboxylic acid, an inhibitor of carnitine palmitoyltransferase I and mitochondrial fatty acid oxidation, inhibits the oxidation of phytanic acid in rat tissues (liver and cultured skin fibroblasts), whereas it has no effect on the oxidation of phytanic acid in human tissues (liver and cultured skin fibroblasts). The higher specific activity of phytanic acid oxidation in peroxisomes compared with that in mitochondria and the endoplasmic reticulum from human tissues and the inhibition of phytanic acid oxidation by 2-[5-(4-chlorophenyl)pentyl]oxiran-2-carboxylic acid in rat tissues (but not human tissues) demonstrate clearly that, in human tissues, phytanic acid is predominantly oxidized in peroxisomes.
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PMID:Phytanic acid alpha-oxidation. Differential subcellular localization in rat and human tissues and its inhibition by nycodenz. 848 24

Changes in selected enzyme parameters were followed in a one year-long toxicologic experiment on albino rat males given vanadium by mouth at either of two dosages: 0.005 mg/kg b.w., which is the equivalent of the regulated level for 1st category drinking water, or 0.01 mg/kg, i.e., twice the safety standard. The endpoints measured included: free sulfhydryl groups in blood serum, heart, and liver; cholinesterase and creatine kinase activities in blood serum; catalase activity in blood; and cytochrome oxidase activity in liver and heart. Chronic oral exposures to vanadium 0.01 mg/kg and, to a lesser extent, 0.005 mg/kg were observed to produce disturbances in redox processes and tissue respiration. The evidence from this study should be taken into consideration when regulating vanadium levels in drinking water from a hygiene standpoint.
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PMID:[An experimental study of the effect of vanadium on enzyme indices in chronic oral exposure]. 852 48

The livers of 13 Sika deer (Cervus nippon Temminck) aged 4 to 9 years and suffering from copper deficiency (enzootic ataxia) were examined histologically, histochemically and by electron microscopy. In addition, the serum and liver copper concentrations, measured in three animals, were found to be low. Histologically, the hepatocytes exhibited cloudy swelling, and numerous haemosiderin deposits were seen in the hepatocytes and Kupffer cells. Staining with p-dimethyl amino-benzylidene-rhodamine revealed distinctly fewer copper granules than normal. Histochemically, 3,3'-diaminobenzidine-H2O2 staining revealed increased numbers of catalase-positive granules around nuclei. Electron microscopically, "giant" and bizarre-shaped mitochondria, irregular depression of the mitochondrial membrane, and fusion of cristae were noted. Disorders of copper-containing enzymes, including cytochrome oxidase, caeruloplasmin and monoamine oxidase, may have been responsible for the mitochondrial abnormalities.
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PMID:Ultrastructure of hepatocytes in copper-deficient Sika deer (Cervus nippon Temminck). 876 86

Some protozoa of the Trypanosomatidae family harbor in their cytoplasm bacterial endosymbionts that provide essential nutrients to and induce morphological alterations in the protozoa. In the present study, a close association between endosymbionts and glycosomes, a peroxisome-like organelle where most of the enzymes of the glycolytic pathway are compartmentalized, was identified by conventional transmission electron microscopy in Crithidia deanei. Such an association was further supported by the cytochemical localization of catalase in the glycosome and also confirmed by 3-D reconstruction of the protozoan. The enzymes cytochrome oxidase and succinate dehydrogenase were detected by ultrastructural cytochemistry. A positive reaction was observed in the protozoan mitochondrion but not in the endosymbiont envelope. Enzymatic assays for succinate cytochrome c reductase reinforced these results, as a low enzymatic activity was detected in an endosymbiont-enriched fraction, while high activity was observed in a purified protozoan mitochondrion fraction. We also demonstrated that a purified symbiont fraction was able to hydrolyze ATP. This activity was Mg+2 dependent, since it was highly stimulated by the presence of physiological concentrations of this ion. Taken together, these observations suggest that no electron transporting system is active in the symbionts of Crithidia deanei and that they might obtain energetic molecules derivated from the protozoan glycosomes.
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PMID:Ultrastructural and biochemical analysis of the relationship of Crithidia deanei with its endosymbiont. 912 37

We propose the name Pseudomonas monteilii for a new species of gram-negative, rod-shaped, motile bacteria that were nonhemolytic on blood agar and were isolated from clinical sources. The 10 strains of P. monteilii were incapable of liquefing gelatin. They grew at 10 degrees C but not at 41 degrees C, produced fluorescent pigments, catalase, and cytochrome oxidase, and possessed the arginine dihydrolase system. They were capable of respiratory but not fermentative metabolism. They did not hydrolyze esculin or starch and were able to use benzylamine, alpha-aminobutyrate, D-ribose, L-arabinose, butyrate, valerate, isovalerate, isobutyrate, inositol, phenylacetate, D-alanine, and amylamine. They possessed L-phenylalanine arylamidase, L-lysine arylamidase, L-alanine arylamidase, gamma-glutamyl-transferase, glycyl-phenylalanine arylamidase, L-tryptophan arylamidase, glycyl-L-alanine arylamidase, esterase C4, esterase C6, esterase C8, esterase C9, esterase C10, and esterase C18. DNA relatedness studies revealed that P. monteilii strains formed a homogeneous DNA hybridization group. A total of 57 strains representing previously described or partially characterized taxa belonging to the genus Pseudomonas were 6 to 54% related to P. monteilii. The highest hybridization values were obtained with strains belonging to or related to Pseudomonas putida biovar A. The average G+C content of the DNA was 60.5 +/- 0.5 mol% for four of the P. monteilii strains studied. The type strain of P. monteilii is CFML 90-60 (= CIP 104883); it was isolated from bronchial aspirate and has a G+C content of 60 mol%. The clinical significance of these organisms is not known.
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PMID:Pseudomonas monteilii sp. nov., isolated from clinical specimens. 922 17

Copper is an essential trace element and has profound influence on cardiac myopathy and heart metabolism. Dietary Cu restriction in rats results in cardiomyopathy, and affects the integrity of the basal lamina of cardiac myocytes and capillaries. Decreased levels of delta subunits of ATP synthetase and nuclear encoded subunits of cytochrome oxidase system have been observed. Alteration in expression of glutathione peroxidase and catalase in heart and liver in Cu deficiency (Cu-) has been noted involving both transcriptional and post transcriptional mechanisms. A short description of two genetically inherited disorders of Cu metabolism, i.e. Wilson's disease and Menkes' disease, and Indian childhood cirrhosis (environmental and/or genetic) have been included to illustrate that advances in the knowledge of Cu cellular transport gives a better understanding of the molecular basis of the pathophysiology of these diseases. Menkes' disease, a human model of defective Cu transport and Cu- has shown many pathological changes, similar to those of heart disease in Cu-. The recent cloning of four genes of putative Cu pumping ATPases (Cu-ATPases) from widely different sources, i.e. two from Enterococcus hirae and one each from Wilson's and Menkes disease patients (which are defective in Cu transport and metabolism), has opened a new chapter in the study of Cu cellular transport and metabolism. The encoded gene products, i.e. Cu-ATPases, show extensive homology and are members of a new class of ATP-driven Cu pumps involved in regulation of cellular Cu. Further, Cu transport by Cop B-ATPase (E. hirae) in membrane vesicles and in isolated rat liver plasma membrane has provided biochemical evidence of its role in ATP-driven Cu transport. In this short review I have critically examined the current evidence of the molecular basis of the pathophysiology of cardiomyopathy in Cu- and, have indicated the possible role of P-type Cu ATPase which may be one of the obligatory factors contributing to cardiomyopathy in experimental animals and probably humans. Experimental verification of this hypothesis will be the aim of future studies.
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PMID:Copper deficiency and heart disease: molecular basis, recent advances and current concepts. 945 22

We examined cell fixation with microwave irradiation (MWI) used in cytochemistry. MWI was applied to blocks of about 1 mm3 of mouse parotid glands at 500 W for about 5 sec in a fixative at 37 degrees C. The activities of endogenous peroxidase and mitochondrial cytochrome oxidase were demonstrated by using the DAB method with 3,3'-diaminobenzidine (DAB) and 0.01% H2O2. Under electron microscopy, peroxidase activity was localized in the nuclear envelope, endoplasmic reticulum and secretory granules. However, mitochondria cytochrome oxidase activity seemed to be rather weak against the MWI at 37 degrees C. Moreover, suspension of isolated hamster liver mitochondria was fixed by MWI and also demonstrated cytochrome oxidase activity by using the cytochemical methods with DAB, cytochrome c, catalase and sucrose. Such mitochondrial fractions were subjected to 6-second MWI given 10 or 18 times with an interval of 10 seconds with and without a chilled water bath. The final temperature of each fixative was kept at about 10 degrees C or rose to about 37 and 55 degrees C. When we took care to keep the temperature below 10 degrees C, the DAB reaction products accumulated in the mitochondrial intermembrane-intracristal space. No mitochondrial deposits were observed when the temperatures of the fixatives rose to 37 and 55 degrees C. These results indicated that peroxidase was very resistant to the heat with MWI fixation. Cytochrome oxidase is sensitive to the heat with MWI, so, a chilled water bath had to be used.
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PMID:Mitochondrial fixation for the detection of cytochrome oxidase activity using microwave irradiation. 958 12

Acrylonitrile (ACN) produces tumors in rats, particularly gliomas of the brain, but tests for genotoxicity have yielded mixed results and no ACN-DNA adducts have been identified in the brain. To examine the possibility that ACN-related brain tumors were not a consequence of binding of ACN to brain DNA, experiments were conducted to investigate possible epigenetic mechanisms. Male Sprague-Dawley rats were exposed to 0, 3, 30, and 300 ppm ACN in drinking water for 21 days, a range that includes doses associated with brain tumorigenesis. In the 30 and 300 ppm ACN groups, 8-oxodeoxyguanosine (8-oxodG) levels were two fold greater than in the controls. Measures of glutathione levels, glutathione peroxidase and catalase were not significantly changed, but cyst(e)ine was somewhat increased. No changes were found in brain cytochrome oxidase activity, which indicates a lack of metabolic hypoxia. Also, no effects on thiobarbituric acid reactive substances were found, indicating a lack of lipid peroxidation. In an additional experiment, male Sprague-Dawley rats were exposed to 0 or 100 ppm ACN in drinking water for 94 days; interim sacrifices were conducted at 3, 10, and 31 days. Levels of brain nuclear DNA 8-oxodG were significantly increased in ACN-exposed rats compared with controls. Another group of animals were given weekly i.v. injections of 5 mg/kg methylnitrosurea and no increases in 8-oxodG were found. These studies suggest the possibility that ACN-induced tumors may be produced by a mode of action involving 8-oxodG. The formation of 8-oxodG is not understood, but does not appear to involve lipid peroxidation or disruption of antioxidant defenses.
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PMID:Formation of 8-oxodeoxyguanosine in brain DNA of rats exposed to acrylonitrile. 970 82


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