Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cytochrome oxidase, glycerol-3-phosphate dehydrogenase, and succinate dehydrogenase were measured in mitochondrial fractions obtained from rat soleus muscle of control and 8 week T3 + T4 treated animals. Under these conditions of prolonged treatment, there is a five-fold increase in the specific activities of both cytochrome oxidase and glycerole-3-phosphate dehydrogenase. Significant increases in total cellular mitochondrial content and enzyme activities were observed in T3 + T4 treated animals as compared to controls. These results indicate that thyrotoxicosis can induce selective changes in mitochondrial enzymes in slow twitch red (Type I) muscle fibers.
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PMID:Effects of thyrotoxicosis on mitochondrial enzymes of rat soleus. 22 61

Expression of the gene for the brown-fat specific uncoupling protein thermogenin was investigated in cell cultures by hybridization of isolated RNA with a cDNA clone corresponding to mouse thermogenin. The RNA was isolated 3-4 days after confluence from cells differentiated in culture from precursors isolated from the interscapular brown adipose tissue of 5-week-old mice. Very low thermogenin mRNA levels were found in cells derived from untreated mice, and there was only little effect of added norepinephrine on thermogenin gene expression in these cells. However, in cells derived from hypothyroid (methimazole-treated) mice there was a higher expression of thermogenin, and norepinephrine had a marked augmenting effect on the thermogenin mRNA level in these cells. These effects of thermogenin mRNA levels were specific, in that they contrasted with the effects of hypothyroidism and norepinephrine on the level of other mRNA species in these cells (coding for beta-actin, lipoprotein lipase, cytochrome-c oxidase, and glycerol-3-phosphate dehydrogenase). It was concluded that brown-fat cells in culture can reach a differentiated state, sufficiently advanced that the unique properties of these cells can be expressed, and that thermogenin gene expression (i.e., the level of thermogenin mRNA) is under direct control of norepinephrine.
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PMID:Brown adipocytes differentiated in vitro can express the gene for the uncoupling protein thermogenin: effects of hypothyroidism and norepinephrine. 249 23

Some metabolic indicators of thyroid hormone activity have been investigated in rats fed on either protein-deficient or energy-restricted diets. Rats were divided into three groups. Control animals were maintained on a diet of protein energy: total energy (P:E) value of 0.20, while the low-protein group (LP) were allowed ad lib. access to food of P:E 0.03. Energy-restricted (ER) rats were given limited amounts of a control diet (P:E 0.20) such that their rate of growth matched that of LP animals. Animals fed on the LP diet had elevated plasma concentrations of both total and free triiodothyronine (T3) concentrations whereas those on the ER regiment showed values below those of controls. The activities of mitochondrial alpha-glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) and of the alpha-glycerol-3-phosphate shuttle system were elevated in the liver of LP rats, but malate-aspartate shuttle operation was reduced. All three activities were reduced in ER animals. Cytochrome c oxidase (EC 1.9.3.1) activity of brown adipose tissue indicated a high rate of thermogenic activity in this tissue in LP rats, but ER animals showed some evidence of below normal function. The results indicate that both the raised plasma T3 of LP rats and the reduced levels observed in ER animals are physiologically significant.
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PMID:Evidence suggesting that the elevated plasma triiodothyronine concentration of rats fed on protein deficient diets is physiologically active. 390 23

Crossed immunoelectrophoresis was used to analyze the components of membrane vesicles of anaerobically grown Escherichia coli. The number of precipitation lines in the crossed immunoelectrophoresis patterns of membrane vesicles isolated from E. coli grown anaerobically on glucose plus nitrate and on glycerol plus fumarate were 83 and 70, respectively. Zymogram staining techniques were used to identify immunoprecipitates corresponding to nitrate reductase, formate dehydrogenase, fumarate reductase, and glycerol-3-phosphate dehydrogenase in crossed immunoelectrophoresis reference patterns. The identification of fumarate reductase by its succinate oxidizing activity was confirmed with purified enzyme and with mutants lacking or overproducing this enzyme. In addition, precipitation lines were found for hydrogenase, cytochrome oxidase, the membrane-bound ATPase, and the dehydrogenases for succinate, malate, dihydroorotate, D-lactate, 6-phosphogluconate, and NADH. Adsorption experiments with intact and solubilized membrane vesicles showed that fumarate reductase, hydrogenase, glycerol-3-phosphate dehydrogenase, nitrate reductase, and ATPase are located at the inner surface of the cytoplasmic membrane; on the other hand, the results suggest that formate dehydrogenase is a transmembrane protein.
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PMID:Identification and localization of enzymes of the fumarate reductase and nitrate respiration systems of escherichia coli by crossed immunoelectrophoresis. 621 54

Young rats were made iron deficient by feeding them a low-iron diet for 8 wk. Iron deficiency resulted in a 50% decrease in cytochrome c and cytochrome oxidase and a 26% decrease in mitochondrial glycerol-3-phosphate dehydrogenase activity in skeletal muscle. Respiratory capacity of muscle homogenates was reduced 55%. After 8 days of iron treatment, respiratory capacity, cytochrome c, cytochrome oxidase, and glycerol-3-phosphate dehydrogenase had returned 50% toward normal. Maximum O2 uptake of contracting hindlimb muscles averaged 8.5 mumol O2.min-1.g-1 in control, 4.3 mumol O2.min-1.g-1 in iron-deficient, and 6.2 mumol O2.min-1.g-1 in the 8-day-iron-repleted rats. Muscle fatigue during 10 min of stimulation was greater in the iron-deficient group. Lactate concentration in red muscle was higher in iron-deficient than in control rats after stimulation. The muscle fatigue and lactate responses returned 50% toward normal during 8 days of iron treatment. We conclude that iron deficiency results in a decrease in skeletal muscle capacity for aerobic metabolism and, by this mechanism, increases susceptibility to fatigue.
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PMID:Physiological and biochemical effects of iron deficiency on rat skeletal muscle. 626 4

Clinical symptoms of acute carbon monoxide (CO) poisoning are mainly related to the capability of haemoglobin to bind CO. However, the persistence of some clinical alterations after carboxyhaemoglobin normalization suggests that other heme containing proteins, like cytochrome c oxidase, could play a role in its pathogenesis. We studied mitochondrial enzyme activities of lymphocytes from three patients suffering from acute CO poisoning. HbCO levels were 11.6%. 19.6% and 22.3% in the acute phase, 2.3%, 2.4% and 1.5% on day 3 after admission, and 1.2%, 3.3% and 1.1% on day 12. Complex II, III and glycerol-3-phosphate dehydrogenase activities remained normal along the study, while cytochrome c oxidase (complex IV) activity showed a 76% inhibition compared to controls during acute poisoning (P < 0.01) and 48% at day 3 (P < 0.05). The activity was normal already on day 12 after the complete disappearance of symptomatology. Our results suggest that mitochondrial cytochrome c oxidase is also a target site in human acute CO poisoning, and its extended and generalized inhibition could explain the persistence of different symptoms after the normalization of HbCO levels.
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PMID:Mitochondrial cytochrome c oxidase inhibition during acute carbon monoxide poisoning. 958 35

Mitochondria constitute a source of reactive oxygen species. We tested whether mitochondrial function from human circulating lymphocytes is affected by smoking habit and if this could be associated with an increase in oxidative damage of biological membranes. We prospectively studied 35 smokers and 35 non-smoking healthy individuals matched by age and sex, with a similar physical activity. Individual enzyme activity of complexes II, III and IV of the mitochondrial respiratory chain (MRC) and of glycerol-3-phosphate dehydrogenase activity were measured spectrophotometrically. Intact cell respiration and oxidative rates after addition of pyruvate, succinate and glycerol-3-phosphate were assessed polarographically. Lipid peroxidation of biological membranes was assessed measuring the loss of cis-parinaric acid fluorescence. Results are expressed as means (+/-SD). Smokers showed a significant decrease in complex IV activity compared with non-smokers (112.8 +/- 40.9 versus 146.4 +/- 62.5 nmol/min/mg protein, respectively; 23% of inhibition; P = 0.01), while the rest of the complexes of MRC were unaffected. Conversely, oxidative rate with succinate, but not with the other substrates, was enhanced in smokers compared with non-smokers (16.7 +/- 10.4 versus 11.4 +/- 4.7 nmol oxygen/min/mg protein, respectively; 46% of activation; P = 0. 01). Lipid peroxidation of lymphocyte membranes was increased in smokers with respect to non-smokers (3.49 +/- 1.27 versus 4.39 +/- 1. 76 units of fluorescence/mg protein, respectively; 21% of increase; P = 0.03) and this increase correlated positively with succinate oxidation activation (R = 0.34, P = 0.02) and, to a lesser extent, with complex IV inhibition, although it did not reach statistical significance (R = 0.19, P = 0.18). In smokers, the MRC function of lymphocytes is disturbed and correlates with the degree of oxidative damage of membranes. This mitochondrial dysfunction could contribute to increased endogenous production of reactive oxygen species and could play a role in tobacco carcinogenicity.
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PMID:Smoking disturbs mitochondrial respiratory chain function and enhances lipid peroxidation on human circulating lymphocytes. 1038 8

To investigate the effects of HIV infection on mitochondrial DNA (mtDNA) content and other mitochondrial parameters, we used peripheral blood mononuclear cells (PBMCs) from 25 asymptomatic antiretroviral-naive human immunodeficiency virus (HIV)-infected patients and from 25 healthy control subjects. HIV-infected patients had significant decreases in mtDNA content (decrease, 23%; P<.05) and in the activities of mitochondrial respiratory chain (MRC) complex II (decrease, 41%; P<.001), MRC complex III (decrease, 38%; P<.001), MRC complex IV (decrease, 19%; P=.001), and glycerol-3-phosphate dehydrogenase (decrease, 22%; P<.001), along with increased lipid peroxidation of PBMC membranes (P=.007). Therefore, HIV infection is associated not only with mtDNA depletion, but also with extensive MRC disturbances and increased oxidative damage.
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PMID:Mitochondrial effects of HIV infection on the peripheral blood mononuclear cells of HIV-infected patients who were never treated with antiretrovirals. 1573 31

In order to investigate the metabolic regulation in Atlantic salmon fries (Salmo salar L.) during their growth, development, and in the course of size divergence, age-related changes in the activity of enzymes involved in the energy and carbohydrate metabolism, including myosin heavy chain isoform expression, RNA/DNA ratio in the white muscles and liver of specimens at ages of 0+; 1+, and 2+, as well as correlations of these characteristics with the body weight of fish specimens were analyzed. Multidirectional changes in the activity of enzymes taking part in aerobic and anaerobic energy metabolism, as well as a decrease in the protein synthesis with age, were revealed. There was a positive correlation between the activities of cytochrome oxidase, lactate dehydrogenase, aldolase, and myosin gene expression in the muscles, cytochrome oxidase activity, glucose-6-phosphate dehydrogenase, and glycerol-3-phosphate dehydrogenase in the liver with the body weight of salmon specimens within the age groups.
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PMID:[Activity of Enzymes Involved in the Energy and Carbohydrate Metabolism and the Level of Some Molecular-Genetic Characteristics in Young Salmons (Salmo salar L.) with Different Age and Weight]. 2660 25