Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.41 (isocitrate dehydrogenase)
 3,101 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This paper reports the time course of development of the intramitochondrial cholesterol side-chain-cleavage activity, cytoplasmic NADP+-dependent isocitric dehydrogenase, malic enzyme and glucose-6-phosphate dehydrogenase during ovarian maturation, using as a model the immature rat ovary stimulated to develop with pharmacological doses of gonadotrophin. These enzymic activities were correlated with increases in ovarian content of DNA, cellular content of adenosin 3':5'-monophosphate, and the levels of plasma progesterone. The plasma progesterone concentrations followed closely the development of the [4-14C]cholesterol side-chain-cleavage which was mimicked by the cytoplasmic isocitric dehydrogenase; both enzymes increased in activity 28 times during the 6 days of this study. There was no correlation between adenosine 3':5'-monophosphate levels and cholesterol side-chain cleavage or progesterone plasma concentrations.
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PMID:Changes in enzyme activities during the artificially stimulated transition from follicular to luteal cell types in rat ovary. 20 54

Controls of fatty acid synthesis in bovine adipose tissue were investigated. Six Brown Swiss steers were fasted for 8 days and then refed for 56 days. Biopsy samples of backfat adipose tissue were taken during the fasting and refeeding periods. Rates of acetate incorporation into fatty acids (FAS), activities of acetyl CoA carboxylase (CBX), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and NADP:isocitrate dehydrogenase, and plasma free fatty acids (FFA) and plasma acetate were determined. FAS decreased 60% after 1 day of fasting and 99% after 8 days. FAS did not increase until day 3 of refeeding when energy intake was above maintenance, then returned to normal by 14 days. CBX followed a pattern similar to FAS, except its activity did rise above the control rate during refeeding. Plasma FFA increased 350% and acetate decreased 67% during fasting. After 4 days of refeeding, FFA returned to normal, and acetate increased to 156% of initial concentration, then returned to normal by 21 days. These data suggest that CBX limits FAS in adipose tissue of cattle.
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PMID:Changes in fatty acid synthesis and lipogenic enzymes in adipose tissue from fasted and fasted-refed steers. 23 91

In an effort to demonstrate biochemical changes occuring in malperfused retinas, oxygen-induced retrolental fibroplasia was produced in kittens. Immediately before the onset of vasoproliferations, that is in the stage of maximal hypoxia, the activities of lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PDH), malate dehydrogenase (MDH) and isocitrate dehydrogenase (ICDH) were determined. The activity of MDH was found to be significantly decreased, whereas the activities of the other enzymes showed no major changes.
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PMID:Retinal enzyme activities under hypoxic conditions prior to neovascularization. 30 9

Mycotoxic porcine nephropathy was induced by p.o. administration of crystalline ochratoxin A for periods of 5 days, 3 months and 2 years. Enzyme activities of the renal tissue were studied histochemically. These were NADH-tetrazolium reductase, NADPH-tetrazolium reductase, lactate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, glucose-6-phosphate dehydrogenase, alpha-glycerophosphate dehydrogenase, unspecific acid phosphatase and unspecific alkaline phosphatase. The activity of NADH-tetrazolium reductase and succinate dehydrogenase was reduced in the proximal tubule of all nephrons after 5 days ochratoxin A exposure and remained reduced after 3 months and 2 years exposure. The effect of ochratoxin A on these enzymes would appear to cause the impairment of proximal tubular function and the morphological changes observed in the proximal tubule in ochratoxin A-induced mycotoxic porcine nephropathy. The localization of alterations in enzyme activity corresponds to the localization of ochratoxin A previously demonstrated in the kidney. The activities of NADPH-tetrazolium reductase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase and unspecific alkaline phosphatase were reduced focally corresponding to the areas with focal tubular atrophy and the degree of reduction was roughly parallel to the degree of atrophy.
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PMID:Ochratoxin A-induced mycotoxic porcine nephropathy: alterations in enzyme activity in tubular cells. 47 26

Enzyme histochemical techniques were applied to frozen sheep uteri from different stages of the oestrous cycle. The localization and activities of succinate, lactate, glucose-6-phosphate, and isocitrate (NADP+) dehydrogenases and acid and alkaline phosphatases were studied in the luminal and glandular epithelia, caruncle and myometrium. Enzyme activity in the sections was scored on a scale of 0--5. In general the enzyme activity in the uterine caruncles and epithelia was higher than in the myometrium. The myometrium did not show any alkaline phosphatase activity and isocitrate dehydrogenase (NADP+) activity was negligible. The low activities of acid phosphatase and lactate dehydrogenase and the moderate levels of glucose-6-phosphate and succinate dehydrogenases in the myometrium were constant. The caruncular tissue showed high levels of phosphatases and glucose-6-phosphate dehydrogenase, moderate levels of lactate and succinate dehydrogenases, and low levels of isocitrate dehydrogenase (NADP+) throughout the oestrous cycle. Much lower phosphatase and isocitrate dehydrogenase (NADP+) levels were found in the epithelium of deep glands compared with superficial glands. The high activity of acid and alkaline phosphatases in the luminal epithelium and the superficial glands was constant from mid-cycle to ovulation, but a significant decrease was observed immediately after ovulation. The level of dehydrogenases in epithelia was generally high and did not change during the oestrous cycle.
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PMID:Enzyme histochemistry of the sheep uterus during the oestrous cycle. 54 17

Electrophoretic variants at four additional enzyme loci--two esterases (Est-2, Est-3), retinal lactate dehydrogenase (LDH-1) and mannose phosphate isomerase (MPI)--among three species and four subspecies of fish of the genus Xiphophorus were observed. Electrophoretic patterns in F1 hybrid heterozygotes confirmed the monomeric structures of MPI and the esterase and the tetrametric structure of LDH in these fishes. Variant alleles of all four loci displayed normal Mendelian segregation in backcross and F2 hybrids. Recombination data from backcross hybrids mapped with Haldane's mapping function indicate the four loci to be linked as Est-2--0.43--Est3--0.26--LDH-1--0.19--MPI. Significant interference was detected and apparently concentrated in the Est-3 to MPI region. No significant sex-specific differences in recombination were observed. This group (designated linkage group II) was shown to assort independently from the three loci of linkage group I (adenosine deaminase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase) and from glyceraldehyde-3-phosphate dehydrogenase and two isocitrate dehydrogenase loci. Evidence for conservation of the linkage group, at least in part, in other vertebrate species is presented.
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PMID:Polymorphisms, linkage and mapping of four enzyme loci in the fish genus Xiphophorus (Poeciliidae). 54 75

To determine the effect of chronic alcohol ingestion, rats were given 15 or 25% v/v of alcohol in water for a period of 6 months. The activities of some key enzymes involved in the metabolism of glucose, mitochondrial respiratory rates, and efficiency of oxidative phosphorylation were studied in the hearts of alcohol-treated and untreated rats. In the group receiving 15% alcohol, glucose-6-phosphate dehydrogenase (G-6-PDH) was elevated. In rats given 25% alcohol, activities of G-6-PDH, aldolase, and glyceraldehyde phosphate dehydrogenase were elevated but isocitrate dehydrogenase was reduced. Mitochondrial respiratory rates and the efficiency of phosphorylation were depressed in rats given 25% of alcohol. Except for mitochondrial oxidation of pyruvate and alpha-ketoglutarate, all biochemical parameters studied were within normal limits a month after alcohol was discontinued.
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PMID:The effect of chronic ethanol ingestion on myocardial glucose and energy metabolism. 56 91

Phenotype and gene frequencies are presented for eight polymorphic systems among the Nubians of South Egypt, namely, acid phosphatase, glucose-6-phosphate dehydrogenase, adenylate kinase, 6-phosphogluconate dehydrogenase, esterase D, phosphoglucomutase I, peptidase A, and haptoglobin. Eleven systems, namely, albumin, ceruloplasmin, hemoglobin, lactate dehydrogenase, isocitrate dehydrogenase, phosphohexose isomerase, malate dehydrogenase, peptidase B and C, phosphoglucomutase II, and transferrin were found to be monomorphic. A single electrophoretic variant of phosphohexose isomerase were observed.
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PMID:The Nubians of Kom Ombo: serum and red cell protein types. 61 20

In this communication the results of applying various histochemical semipermeable membrane techniques to the localization of several enzymes in bovine and porcine heart are presented. The Purkinje fibers of the atrioventricular conducting system of the bovine heart differ from the myocardium proper in containing a greater activity of the glycolytic and gluconeogenetic enzymes--lactate dehydrogenase, glyceraldehyde-phosphate dehydrogenase, hexokinase, glucosephosphate isomerase and phosphoglucomutase, and less activity of the aerobic enzymes--NADH: nitroBT oxidoreductase and isocitrate dehydrogenase (NADP+). The metabolic reactions obtained with Purkinje fibers of the porcine heart are less pronounced. These histochemical findings are in accordance with the impression that Purkinje fibers, compared with the common myocardial fibers, have a higher rate of anaerobic metabolism and a lower rate of aerobic metabolism. The activity of the NADPH regenerating enzymes glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating), and the activity of acid hydrolases such as non-specific esterase and acid phosphatase is higher in the Purkinje fibers of both the bovine and porcine heart.
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PMID:Enzyme histochemical studies on the Purkinje fibers of the atrioventricular system of the bovine and porcine hearts. 66 82

The activities of twelve enzymes were measured in crude extracts from cells of Escherichia coli K-10 grown aerobically or anaerobically in a defined medium in the presence or absence of nitrate. The activities of isocitrate dehydrogenase, aconitate hydratase, 2-oxoglutarate dehydrogenase, malate dehydrogenase, malic enzyme, and D-lactate dehydrogenase (NAD+-independent) were found to be higher in cells grown in nitrate respiration than in those in fermentation, but lower than in those in respiration. This finding may explain the incomplete oxidation in nitrate respiration and, on the other hand, suggests the operation of the tricarboxylic acid even under these conditions. The activities of succinate dehydrogenase and alcohol dehydrogenase in relation to the formation of fermentation product were as high in cells grown in fermentation as in those in respiration and were low in those in nitrate respiration. However, that ratio of the activities in the latter case to the activities in respiration was the same as the ratio for most enzymes in the tricarboxylic acid cycle. The level of lactate dehydrogenase (NAD+-dependent) was not affected by nitrate respiration but its activity in the extract was inhibited by nitrate and nitrite. The absence of lactate in the anaerobic culture with nitrate may be due to this inhibition as well as NADH oxidation by nitrate. Levels of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were not altered by the growth conditions and that of pyruvate dehydrogenase was low only in cells grown in fermentation.
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PMID:Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. 77 52


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