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)

The aim of the present study was to evaluate the effects of medroxyprogesterone acetate (MPA), an inducer of liver drug metabolism, on the ability of liver to generate NADPH, a reducing cofactor for drug oxidation reactions in normal rats and to compare these results with those obtained in rats receiving phenobarbital (PB), a well known inducer of liver drug metabolism. The results showed that: 1. Administration of MPA (100 mg/kg body wt) for a week increased liver wt and NADPH cytochrome P-450 reductase activity, suggesting that the compound induced liver drug metabolism. 2. The regimen also increased the activities of two NADPH generating enzymes, isocitrate dehydrogenase and malic enzyme, suggesting that MPA enhanced the capacity of normal liver tissue to produce NADPH. 3. Phenobarbital treatment increased the activities of three NADPH generating enzymes, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and malic enzyme, suggesting that MPA and PB differ in their effects on the liver NADPH-producing system.
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PMID:Medroxyprogesterone acetate (MPA) enhances liver NADPH-generating enzyme activities in normal rats. 297 Sep 86

The administration of medroxyprogesterone acetate (MPA) and phenobarbital (PB) improves liver function in rats with liver damage. This was seen here as increased aryl hydrocarbon hydroxylase (AHH) activity after therapy with MPA or PB in rats with a chemical liver injury, produced by dimethylnitrosamine (DMN). Hepatic glucose-6-phosphatase (G6Pase) activity, an index of glucose metabolism was also normalized in the MPA treated rats. The present study further shows that MPA induced hepatic malic enzyme (ME) and isocitrate dehydrogenase (ICDH) activities and PB enhanced glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH) and ME activities in the DMN pretreated rats. This suggests that MPA and PB enhanced the capacity of altered liver tissue to generate NADPH, a cofactor in the monooxygenase system, which may, in part, enhance the restoration of drug hydroxylation in the rats. Since G6PDH, 6PGDH and ME participate in glucose metabolism, the finding that the compounds influenced these enzymes in distinct ways, may explain the different effects of MPA and PB on the restoration of glucose metabolism.
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PMID:Medroxyprogesterone acetate and phenobarbital induce NADPH producing enzyme activities in rats with a chemical liver injury. 300 83

The present study was conducted on bone tissue responses to irradiation towards a treatment model of mandibular irradiation injury by comparing the results of experimental observations of irradiation effects on rabbit hind legs and rat mandibular bones (paper I, II and III) with clinical observations of irradiation effects on the human mandible (paper IV, V and VI). The main results of the study were as follows: Bone marrow haemorrhage, eosinophilia and incipient edema were encountered in the rabbit leg one day after a single irradiation dose. Edema and fibrosis were the salient features after five weeks, while both regenerative and fibrotic changes predominated eleven weeks after irradiation. The changes were the more extensive the greater the irradiation dose was. Empty lacunae as a sign of cell damage in cortical bone already appeared on the first day after irradiation; this effect reached its maximum when the dose was 20 Gy or more. Bone marrow and subcutaneous tissue pO2 and pCO2 were measured by means of implanted Silastic tonometers in irradiated and nonirradiated rabbit hind legs. Single dose irradiation was followed by a rapid, dose dependent decrease of marrow pO2. The corresponding effect on pCO2 was weaker and appeared later. The response to hyperoxia in the bone marrow became weaker when the irradiation dose increased. Less significant was the response of CO2 tension to hyperoxia. O2 and CO2 tensions were recovered after single dose irradiation both in subcutaneous tissue and in bone marrow, but the reduction was less in bone marrow. During the twelve weeks observation period clearly better recovery in tissue gas tensions was observed in subcutaneous tissue than in bone marrow. Nonirradiated periosteal grafts on irradiated bone cavities in the rabbit tibia induced more rapid and intense mature bone formation than irradiated periosteal grafts. The irradiated periosteum, even after a single dose of 20 Gy, had some osteogenetic capacity. The alkaline phosphatase content was lowered eight weeks after surgery in irradiated legs but clearly exceeded control values twelve weeks after surgery indicating new bone formation. Lysosomal enzyme DAP II contents were increased in all irradiated specimens as a sign of disturbed bone formation. The tissue concentrations of acid phosphatase, cytochrome oxidase, lactate dehydrogenase, isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase and succinate dehydrogenase in the immediate postirradiation period showed a greater increase in activity in the cut lines of the irradiated rat mandibles than in those of the nonirradiated mandibles.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Bone tissue response to irradiation and treatment model of mandibular irradiation injury. An experimental and clinical study. 309 Aug 54

Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
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PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49

Estradiol treatment modified the metabolic responses of fasted rat hepatocytes to exogenous glucose with respect to glucose utilization and cytosolic NADPH-generating enzymes. The estrogen abolished the glucose-stimulated gluconeogenic capacity displayed by control rat cells while promoting a net uptake of exogenous glucose and enhancing the glucose-6-phosphate dehydrogenase activity. Estradiol also caused an increase in the activity of the isocitrate dehydrogenase that may be related to the enhanced needs of NADPH by hepatocytes for steroid hormone catabolism.
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PMID:Estradiol-produced modifications on the response to glucose of hepatocytes from fasted rats. 319 Sep 24

Testicular lipids act as source of energy, structural components of spermatozoa and precursors of androgen biosynthesis. Treatment with antispermatogeneic agents cause accumulation of testicular lipids. Gossypol, an effective antispermatogenic agent causes marked accumulation of testicular neutral lipids. It did not affect testicular phospholipids. Gossypol treatment did not bring about marked changes in the key enzymes like HMG Co A reductase, glucose-6-phosphate dehydrogenase malic enzyme and cytosolic isocitrate dehydrogenase involved in sterol biosynthesis. Thus, gossypol brings about marked accumulation of glycerides and esterified cholesterol in the testis due to its effect on spermatogenic elements of adult rats.
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PMID:Gossypol and testicular lipids of adult rats. 321 29

Molecular mass, Stoke's radius, frictional coefficient and isomer-type of non-denatured proteins can be obtained by time-dependent gradient gel electrophoresis by evaluating the resulting data using a two-step mathematical procedure. Provided a histochemical staining procedure is available to locate the position of an enzyme in the gel, crude cell extracts can be used for estimating their molecular size properties. The computation of molecular properties of non-denatured proteins is demonstrated for isozymes of aspartate aminotransferase (EC 2.6.1.1), peroxidase (EC 1.11.1.42) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) from current-year needles of spruce. The resulting data as well as those which were calculated for esterase (EC 3.1.1.1), glutamate dehydrogenase (EC 1.4.1.4), isocitrate dehydrogenase (EC 1.4.1.42), and shikimate dehydrogenase (EC 1.1.1.25) are in accordance with those reported in the literature. The method described may be applied to various scientific areas such as genetics or environmental pollution. It could be shown here that current-year needles of injured spruce (damage class 3) contained two more peroxidase isozymes and one more glucose-6-phosphate dehydrogenase isozyme than those from non-injured trees. These differences may mark two genotypes of spruce of different susceptibilities towards present-day air and soil pollutants.
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PMID:Determination of molecular mass, Stokes' radius, frictional coefficient and isomer-type of non-denatured proteins by time-dependent pore gradient gel electrophoresis. 323 69

Acclimation of carp both to the temperature fall (from 20 to 5 degrees C) and rise (from 20 to 30 degrees C) induces an increase in activity of cytoplasmic liver NADPH-generating enzymes--glucose-6-phosphate dehydrogenase (G6PDG) and malic-enzyme (ME) 6-phosphogluconate dehydrogenase (6PGDG) and NADP-isocitrate dehydrogenase (NADP-IDG) activities are unchanged. Actinomycin D does not prevent cold activation of G6PDG but blocks activation of ME. "Warm" G6PDG has minimal Km value for glucose-6-phosphate and "warm" ME has minimal Km value for glucose-6-phosphate and "warm" ME has minimal Km value for malate at 25 degrees C "Cold" G6PDG and ME have the warmest Km values at 5 degrees C. Isozyme composition of cytoplasmic G6PDG (2 bands with Rf 0.16 and 0.20) does not change within the limits of 5-30 degrees C. The prolactin action on G6PDG and ME is similar to the effect of cold acclimation (activity increases Km value decreases, isozyme pattern (for G6PDG) remains unchanged). It is supposed that activation of G6PDG and ME during cold adaptation may be a result of the prolactin action on substrate-binding ability without changes in the enzyme biosynthesis and isozyme pattern.
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PMID:[The effect of temperature acclimation on NADP-dependent dehydrogenase activity in the carp liver and various mechanisms of its regulation]. 323 95

There were significant changes in enzyme activities and concentrations of metabolites in the blood and liver of cows with fatty livers when compared to normal cows. Blood and liver samples were taken from cows at the abattoir immediately after slaughter. The liver was checked for pathological signs and the samples were divided according to the degree of fatty changes. Three groups were studied: controls showing no gross pathological signs, mild fatty infiltration and severe infiltration. In cows with fatty liver, there were significant increases in the serum activities of isocitric dehydrogenase (ICDH), glucose-6-phosphate dehydrogenase (G6PDH), glutamic dehydrogenase (GLDH), lactic dehydrogenase (LDH), malic dehydrogenase (MDH), aspartate aminotransferase (AST), alkaline phosphatase (ALP) and acid phosphatase (ACP). In the fatty liver, the activities of the enzymes, ICDH, G6PDH, LDH, MDH, ALP and malic enzyme (ME) were significantly higher, while sorbitol dehydrogenase (SDH) was significantly lower. While serum total lipid decreased, the opposite was seen in the liver with higher lipid content, mainly due to triglycerides and cholesterol esters. The significant increases in the NADPH generating enzymes ME, ICDH, G6PDH and MDH, which are required for fatty acid synthesis, suggest that the lipids accumulated in the liver are not only of extrahepatic origin, mobilized into the liver, but also arise from increased lipid synthesis in the liver which is induced during the laying down of fat in the liver. Measurement of the serum NADPH generating enzymes may serve as a useful biochemical test specific for fatty liver in cows.
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PMID:Biochemical changes associated with the fatty liver syndrome in cows. 339 48

Cerebral forebrain arterioles and neuropil were analyzed histochemically to determine the effects of chloral hydrate anesthesia on key enzymes of aerobic and anaerobic metabolism, as well as the hexose monophosphate shunt in rats. Significant decreases were observed in cytochrome oxidase, and beta-hydroxybutyrate dehydrogenase in arterioles, while glucose-6-phosphate dehydrogenase and isocitric dehydrogenase showed a significant increase and lactate dehydrogenase showed no significant change. In the neuropil, cytochrome oxidase, isocitrate dehydrogenase and glucose-6-phosphate dehydrogenase showed significant increases following chloral hydrate administration, while beta-hydroxybutyrate dehydrogenase and lactate dehydrogenase showed no significant changes. These data suggest that surgical anesthetic levels of chloral hydrate can impair forebrain metabolism which may lead to altered electrophysiological responses.
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PMID:Chloral hydrate anesthesia alters cerebral enzymes in the rat. A histochemical study. 343 84


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