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Target Concepts:
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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)
In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and
lactate dehydrogenase
, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of
lactate dehydrogenase
predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction,
cytochrome oxidase
, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
...
PMID:Enzymatic organization of the subcommissural organ. 123 49
To study the effects of deep freezing on the energy metabolism of human spermatozoa, we investigated, by cytochemical quantitative methods,
cytochrome oxidase
and
lactate dehydrogenase
activities of fresh and frozen human spermatozoa during in vitro capacitation. Fresh and frozen human spermatozoa were incubated in Biggers, Whitten and Wittingham's medium supplemented with 15% heat-inactivated human serum. Both histoenzymological reactions can be quantitated and have been evaluated by microdensitometric method. The results indicate that human spermatozoa depend almost entirely on anaerobic glycolysis during in vitro capacitation and suggest that both aerobic and anaerobic metabolism in spermatozoa are only slightly impaired by freezing-thawing and storage.
...
PMID:[Cytochemical study of human sperm metabolism during in vitro capacitation after cryopreservation]. 132 25
Human spermatozoa contain appreciable amounts of intracellular glutathione, which has a protective function against peroxidative degradation of spermatozoal polyunsaturated fatty acids by the NADPH-dependent glutathione peroxidase/reductase enzymatic system. The glutathione system provides a basic defense against peroxidative damage, without which the superoxide dismutase system would dominate. Since oxidative damage is said to include enzyme leakage and changes in metabolism,
cytochrome oxidase
and
lactate dehydrogenase
activities were used as indicators of the energy metabolism in unwashed and washed human spermatozoa during lipid peroxidation. Lipid peroxidation was induced by aerobic incubation of sperms in the presence of sodium ascorbate and ferrous sulphate. In addition, since NADPH concentrations influence the concentration of reduced glutathione, we studied glucose-6-phosphate dehydrogenase activity as an indicator of pentose phosphate shunt activity, the main source of NADPH. Microdensitometric measurements of the three enzymes were made by a Vickers M85a scanning microdensitometer. We found that the lipid peroxidation process greatly affects the 3 enzymatic activities examined and that seminal plasma protects against the extensive deleterious effects of lipid peroxidation.
...
PMID:Cytophotometric assay of cytochrome oxidase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activities in human peroxidized spermatozoa. 133 42
Winter- and summer-acclimatized largemouth bass (Micropterus salmoides) were collected from hatchery ponds in eastern Colorado during late winter and midsummer, then challenged with two prolonged swimming performances (step test and constant-velocity endurance). Variation in the step test performances was significantly correlated with variation in the endurance performances in the winter-acclimatized but not in the summer-acclimatized fish. Fourteen physiological and morphological traits were measured on each fish, and correlations among these traits and swimming performance were tested. None of the traits measured were correlated with performance variation in both the winter- and summer-acclimatized fish. The only significant correlate with swimming performance in the summer-acclimatized fish was white muscle
lactate dehydrogenase
activity (n = 19). Six of the seven factors correlating with winter swimming performance (n = 18-19) could be divided into two categories: traits associated with fasting (condition factor and liver enzymatic activity) and those associated with oxygen delivery (heart mass, heart and red muscle
cytochrome oxidase
activity). The results of this study suggest that morphological and physiological correlates of swimming performance in juvenile largemouth bass are profoundly influenced by seasonal variation.
...
PMID:Morphological and physiological correlates with swimming performance in juvenile largemouth bass. 144 21
The influence of tapering on the metabolic and performance parameters in endurance cyclists was investigated. Cyclists (n = 25) trained 5 days.week-1, 60 min.day-1, at 75-85% maximal oxygen consumption (VO2max) for 8 weeks and were then randomly assigned to a taper group: 4D (4 days; n = 7), 8D (8 days; n = 6), CON (control, 4 days rest; n = 6), NOTAPER (non-taper, continued training; n = 6). Muscle biopsy specimens taken before and after training and tapering were analysed for carnitine palmityltransferase (CPT), citrate synthase, beta-hydroxyacyl CoA dehydrogenase (HOAD),
cytochrome oxidase
(CYTOX),
lactate dehydrogenase
, glycogen and protein. Significant increases in VO2max (6%), a 60-min endurance cycle test (34.5%), oxidative enzymes (77-178%), glycogen (35%) and protein (34%) occurred following training. After the taper, HOAD and CPT decreased 25% (P less than 0.05) and 26% respectively, in the CON. Post-taper CYTOX values were different (P less than 0.05) for 4D and 8D compared with CON. Muscle glycogen levels were increased (P less than 0.05) after tapering in the 4D, 8D and CON, but decreased in NOTAPER. Similarly, power output at ventilation threshold was significantly increased in the 4D (27.4 W) and 8D (27 W) groups, but decreased (22 W) in the NOTAPER. These findings suggest that tapering elicited a physiological adaptation by altering oxidative enzymes and muscle glycogen levels. Such an adaptation may influence endurance cycling during a laboratory performance test.
...
PMID:The effects of a reduced exercise duration taper programme on performance and muscle enzymes of endurance cyclists. 150 37
The activities of enzymes related to energy metabolism in the gastrocnemius and soleus muscles in young-adult (4 months), mature (12 months), and senescent (24 months) rats were compared after continuous (72 consecutive h) exposure to normobaric hypoxia or normoxia after the vasodilator naftidrofuryl or saline solution had been given intraperitoneally for 30 consecutive days. The maximum rats (Vmax) of the following enzyme activities in the crude extract and/or the crude mitochondrial fraction of each muscle specimen were evaluated for: the anaerobic glycolytic pathway (hexokinase, phosphofructokinase, pyruvate kinase, and
lactate dehydrogenase
), the tricarboxylic acid cycle (citrate synthase, and malate dehydrogenase), the electron transfer chain (
cytochrome oxidase
), and the NAD+/NADH redox state (total NADH cytochrome c reductase). The significance of differences between the enzyme activities at different ages or under different experimental conditions in the two tissue preparations of the two muscles were determined by ANOVA. MCA and ETA2 were used to evaluate the net effects of the experimental conditions. First, aging did not seem to affect the soleus and gastrocnemius muscles in the same way. In the gastrocnemius muscle, the major changes were seen in enzymes of the glycolytic pathway, in the crude extracts. In the soleus muscle, the more striking changes in enzyme activities as a function of aging were found in the crude mitochondrial fraction. We also found that hypoxia caused more important changes in 12-month-old rats than in those of other ages (especially the enzyme activities of the gastrocnemius muscle). Naftidrofuryl modified the effects of hypoxia only sometimes and further investigations are necessary before we can draw any conclusions about the pharmacological activity of naftidrofuryl in hypoxia.
...
PMID:Effects of hypoxia and pharmacological treatment on enzyme activities in skeletal muscle of rats of different ages. 164 27
The postnatal maturation of
cytochrome oxidase
and
lactate dehydrogenase
activity was assessed by histochemistry in rats at 8 postnatal stages, P0, P5, P10, P14, P17, P21, P35 and the adult stage. Enzyme activities were revealed on cryostat brain sections with diaminobenzidine for
cytochrome oxidase
and nitroblue tetrazolium for
lactate dehydrogenase
. Lactate dehydrogenase activity remained unchanged between P0 and P10, significantly increased in 8 areas of the 14 studied between P10 and P14 and in 6 structures from P14 to P17. These were mainly parietal, auditory and cerebellar cortices, hippocampus, thalamus, hypothalamus and medial geniculate body. There was no further change until P35 and
lactate dehydrogenase
activity increased then significantly to reach higher adult levels in hippocampus and medial geniculate body. Cytochrome oxidase activity was low from P0 to P10 and increased in 8 regions between P10 and P14. These were all cortices, caudate nucleus, hippocampus, inferior colliculus and genu. Enzyme activity further increased between P14 and P17 in auditory cortex, medial geniculate body and brainstem, did not vary from P17 to P21 but increased by 92 to 371% in all areas between P21 and P35. Cytochrome oxidase activity rose further from P35 to adult stage in hippocampus and medial geniculate body. From birth to adulthood,
cytochrome oxidase
activity increased 5 to 19 fold and
lactate dehydrogenase
activity 1.8 to 3.0. The present study shows that there is a quite good correlation between postnatal changes in regional cerebral glucose utilization and activity of enzymes involved in glycolytic and oxidative glucose metabolism in the rat.
...
PMID:Quantitative histochemical changes in enzymes involved in energy metabolism in the rat brain during postnatal development. I. Cytochrome oxidase and lactate dehydrogenase. 166 81
1. Forty-eight pigs weaned at 3 weeks old and acclimated to the experimental temperatures for 2 weeks before the start of the experiment, were fed ad lib and used between 9 and 33 kg live weight to determine the effects of warm exposure (31.5 vs 18.5 degrees C) on adipose tissue and muscle metabolism. 2. Warm exposure induced a decline in the lipid content (P less than 0.01) of backfat whereas degree of saturation (P less than 0.05) and adipocytes size were increased (P less than 0.05). 3. At 31.5 degrees C, as compared to 18.5 degrees C, activities of malic enzyme and glucose-6-phosphate dehydrogenase were depressed by an average 33% in backfat (P less than 0.01) and 23% in leaf fat (P less than 0.05) while lipoprotein-lipase activity was stimulated by 60% (P less than 0.01) in leaf fat. 4. In warm conditions, the activities of the enzymes indicative of oxidative and glycolytic metabolism in muscle, i.e.
lactate dehydrogenase
, beta-hydroxyacyl coenzyme-A dehydrogenase, citrate synthase and
cytochrome oxidase
, were reduced in the longissimus dorsi muscle (P less than 0.05) and to a lesser extent in the trapezius muscle. 5. At 31.5 degrees C, pigs exhibit lower average plasma levels of insulin, T3 and T4 than those maintained at 18.5 degrees C.
...
PMID:Effects of warm exposure on adipose tissue and muscle metabolism in growing pigs. 168 95
A study is performed on the long-term effect of the chloracetanilide herbicide "Acetochlor" in doses 21.0; 10.6: 5.5 and 2.6 mg/kg-1 in conditions of 6-month oral application and 2-month rehabilitation period on the metabolite processes and the balance of the connective-tissue components in the myocardium and aorta of male white rats. A complex of biochemical and histological methods are performed (activity of succinate dehidrogenase,
lactate dehydrogenase
, glucose-6-phosphate dehydrogenase, adenosin triphosphatase,
cytochrome oxidase
, fructoso-1,6-diphosphatase, level of the thiol groups, soluble globular, elastine, collagen fractions, insoluble collagen and elastine, general and sulphated glucosamino glycanes). The dose 21.0 mg/kg-1 leads to blocking of the thyol groups, inactivation of succinate dehydrogenase,
cytochrome oxidase
, adenosin triphosphatase, fructose-1,6-diphosphatase, glucose-6-phosphate dehydrogenase, activation of
lactate dehydrogenase
, decrease of the soluble globular, elastine, and collagen fractions and increase of the glucoseaminoglycanes in the heart muscle and aorta. The changes established in the heart muscle at 10,6 mg/kg-1 certify for stronger sensitivity of the organ of the aorta wall. The presence of single changes in the examined indices, their complete dying out after the rehabilitation period and absence of structural changes in the myocardium and aorta permit the dose of 5.5 mg/kg-1 to be accepted as not effective in the conditions of chronic experiment concerning the cardiovascular system.
...
PMID:[The effect of the acetanilide herbicide Acetochlor on the cardiovascular system of white rats]. 179 94
The presence of a unique inclusion body, the microcylinder, in the intracristal space of mitochondria was previously reported in various types of cells from spotted rats of the Long-Evans strain, but was not found in cells of albino rats. The microcylinder is about 30 nm in diameter and of indefinite length, and is composed of six filamentous subunits surrounding a central one. We performed electron microscopic cytochemical studies on the cells of uriniferous tubules and the corpus striatum in normal spotted rats of the Long-Evans strain and albino rats of Wistar and Sprague-Dawley strains. On the basis of oxidative polymerization of 3, 3'-diaminobenzidine by
cytochrome oxidase
(CYO) an cupric ferrocyanide deposition by monoamine oxidase (MAO), microcylinders were demonstrated to exhibit activity of these enzymes. Reaction products of other mitochondrial enzymes, such as succinate dehydrogenase and
lactate dehydrogenase
, were not deposited on microcylinders. We conclude that microcylinders are rat strain-specific mitochondrial inclusions and consist of protein components, particularly containing the mitochondrial enzymes CYO and MAO.
...
PMID:Ultrastructural localization of cytochrome oxidase and monoamine oxidase on microcylinders, a Long-Evans rat-specific mitochondrial inclusion. 184 58
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