Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8NEX9 (reductase)
 26,410 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extreme endurance training was used to investigate the adaptability of the rat diaphragm muscle fibers. During the final phase of the 14-wk training program, the animals were running for 240 min/day at an estimated requirement of 80% of pretraining maximal O2 consumption. Analysis of a sample of the costal diaphragm indicated that training resulted in a 34% reduction (P less than 0.05) in the percent distribution of type IIa fibers [27.7 +/- 1.1 vs. 18.3 +/- 2.6 (SE)] and a 15% increase (P less than 0.05) in the percent of type IIb fibers (40.0 +/- 1.2 vs. 46.1 +/- 2.4). No change (P greater than 0.05) was found in the distribution of the type I fibers (32.3 +/- 1.2 vs. 35.7 +/- 1.3). Oxidative potential as assessed with NADH-tetrazolium reductase and measured microphotometrically increased (P less than 0.05) by 19% in type I fibers but did not change in either the type IIa or type IIb fibers. No effect of training was found when a different oxidative marker, succinic dehydrogenase, was employed. Similarly glycolytic potential based on the activity of alpha-glycerophosphate dehydrogenase was not affected by training. Glycogen concentration was elevated by 60% (P less than 0.01) in type I fibers and 77% (P less than 0.01) in type IIb fibers with training but was not altered (P greater than 0.05) in type IIa fibers. Reductions (P less than 0.05) in fiber area ranging from 11 to 20% were observed in all fiber types as a result of training, whereas the number of capillaries per fiber remained static.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Extreme endurance training and fiber type adaptation in rat diaphragm. 273 83

The histochemical activities of nonspecific acid and alkaline phosphatases, NADH- and NADPH-tetrazolium reductases, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase were investigated in kidneys from rats treated with lithium and lithium plus neuroleptics. During the first 8 weeks of lithium treatment the activity of NADH-tetrazolium reductase, succinate dehydrogenase and alpha-glycerophosphate dehydrogenase activity in the collecting ducts increased. The other enzymes did not change. After 8 weeks of treatment no further changes in enzyme activity occurred. Withdrawal of lithium caused normalization of enzyme activity after 8 weeks. A decrease in concentration ability was found in parallel with the increase in enzyme activities (p less than 0.001). The changes in enzyme activity were not significantly correlated to morphological changes in the collecting ducts. Treatment with neuroleptics alone caused no change in enzyme activity. During combined lithium plus neuroleptic treatment the enzyme activities changed in a similar way as during lithium therapy, but the changes were less pronounced. In parallel, a less pronounced decrease in concentration ability was found during this treatment.
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PMID:Correlation between distal nephron enzyme activity, structure and function in rats during lithium and lithium plus neuroleptic treatment. 285 95

The effects of thyroid hormone on the NADH-tetrazolium reductase activity (oxidative metabolism marker) of soleus (slow-oxidative) and tensor fascia lata (fast-glycolytic) motoneurons were determined and compared with changes in a variety of enzyme activities in the corresponding muscle fibers. Histochemical assays have demonstrated a selective and qualitative conversion in muscle fiber ATPase and quantitative increases of NADH-tetrazolium reductase (oxidative) and mitochondrial alpha-glycerophosphate dehydrogenase (glycolytic) activities in the soleus muscle. Paralleling the selective action upon the soleus slow muscle fibers was a selective central nervous system effect of thyroid hormone on oxidative enzymes of soleus slow-oxidative motoneurons. This indicates that either thyroid hormones act directly and specifically on slow motoneurons or that conversion of the muscle fibers by thyroid hormones produces secondary changes in the motoneuron. These data strengthen the hypothesis that oxidative enzyme activities in motoneurons are tightly matched with oxidative enzyme activities in muscle fibers.
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PMID:Hyperthyroidism selectively increases oxidative metabolism of slow-oxidative motor units. 295 23

The effects of thyrotropin-releasing hormone (TRH) and its putative metabolite, cyclo-histidine-proline (cHP), on the homeothermic development of neonatal rats were studied. The daily intrathecal administration of 10(-11)-10(-9) moles of TRH during the second week of age produced a significant rise in body temperature by 3 weeks of age and was followed by a transient period of hypothermia. This effect, which could not be produced by an intraperitoneal injection of 10(-7) moles of TRH, was abolished by the simultaneous administration of 6-hydroxydopamine (6OHD). In contrast, intrathecally administered cHP decreased thermogenesis. During TRH treatment, brain norepinephrine (NE) and dopamine (DA) release was accelerated 2- to 4-fold. Two weeks after either TRH or cHP treatment, brain NE and DA were significantly reduced; adrenal NE in cHP-treated rats increased. The weight of the interscapular brown adipose tissue (BAT) was decreased by both cHP and 6OHD. At 3 weeks of age, [3H]guanosine diphosphate binding capacity in BAT mitochondria was reduced by 60% in TRH-treated rats and was associated with reduced mitochondrial levels of alpha-glycerophosphate dehydrogenase and liver cytochrome C reductase. These results indicate that TRH stimulates central NE release thereby enhancing thermogenesis, cHP decreases heat production, and TRH-induced hyperthermia is associated with changes in mitochondrial exothermic processes. The central TRH-cHP system may modulate the maturation of homeothermic mechanism in neonatal rats.
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PMID:Effects of thyrotropin-releasing hormone and cyclo-histidine-proline on the homeothermic development of neonatal rats. 309 34

Comparisons were made of the histochemical characteristics of skeletal muscle from 10 animal species. The basic comparison was made from the staining patterns for the myofibrillar actomyosin ATPase produced by preincubation of fresh frozen cross-sections of muscle at alkaline pH (10.30) or acid pH (4.60) with those produced by preincubation in media containing Cu2+ at alkaline pH (10.30), near neutral pH (7.40), or acid pH (4.60). Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase to provide an indication of the relative oxidative and glycolytic capacity of the different fiber types. Type II fibers in mixed fibered muscles were either very sensitive, moderately sensitive, or relatively insensitive to inactivation of the myofibrillar actomyosin ATPase after acid preincubation. These fibers were identified as type IIA1, IIA2, and IIA3, respectively. The myofibrillar actomyosin ATPase of the type I fibers of these muscles, with the exception of those in mouse muscle, was activated by pretreatment with acid. A separation of animal species was possible based on the stability of the IIA1 fibers to inclusion of Cu2+ in the preincubation medium. For one group of animals (rat, mouse, monkey, man, dog, rabbit, and cow), a reciprocal relationship existed between lability to acid and stability to Cu2+ for type IIA1 and IIA3 fibers, respectively. For the second group of animals (horse, ass, and cat) there was a parallel relationship between lability or stability of the type IIA1 and IIA3 fibers to pretreatment with either acid or Cu2+.
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PMID:Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper. 315 28

The purpose of this study was to determine whether 8-12 wk of endurance training produces biochemical and histochemical adaptations in skeletal muscle in foxhounds. Analyses were performed on samples removed from gastrocnemius, triceps, and semitendinosus muscles of foxhounds before and after a treadmill running program. Biochemical analysis showed that training did not alter the activities of phosphofructokinase, beta-hydroxyacyl-CoA dehydrogenase, succinate dehydrogenase, or total phosphorylase. Histochemical analysis of myofibrillar actomyosin ATPase demonstrated three distinct classes of type II fibers and one type I fiber in the semitendinosus and triceps muscles and two type II and two type I fibers in the gastrocnemius muscle. Fiber type distribution and oxidative and glycolytic potentials, as indicated by nicotinamide adenine dinucleotide tetrazolium reductase or alpha-glycerophosphate dehydrogenase staining intensity, were unaltered by training. Similarly, capillary density, capillary-to-fiber ratios, and capillary area-to-fiber area ratios did not change with training. Thus, unlike humans and other mammals (i.e., rat), these foxhounds did not manifest biochemical or histochemical adaptations in skeletal muscle as the result of endurance training. This is consistent with the results of the study in which endurance training produced a 27% increase in maximal cardiac output and a 4% increase in maximal arteriovenous O2 extraction in foxhounds.
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PMID:Dynamic exercise training in foxhounds. II. Analysis of skeletal muscle. 316 58

Quantitative enzyme histochemical methods have been used to determine the effect of ablation of synergists on the oxidative metabolism of the alpha-motoneurons and muscle fibers of the rat soleus. Sixty days postablation, the NADH-tetrazolium reductase (NADH-TR) activity of soleus motoneurons decreased 12.5% from 0.327 +/- 0.005 (mean +/- SE; optical density units) to 0.286 +/- 0.007. In the muscle fibers, the alpha-glycerophosphate dehydrogenase activity (glycolytic enzyme) decreased from 0.114 +/- 0.010 to 0.074 +/- 0.009, a change of 35.1%, and the NADH-TR activity decreased 21.2% from 0.348 +/- 0.018 to 0.274 +/- 0.017. In both the motoneurons and the muscle fibers, the decrease was nonspecific for all cells, although a greater effect on the cells with higher enzyme activity was observed. The decreased NADH-TR activity represents a shift in the oxidative profile of the motoneurons and muscle fibers, indicating a decreased ability to use oxidative metabolism for periods of short-term high-energy demands. Furthermore, the parallel decrease in muscle fibers and motoneurons with high NADH-TR activity (fast-twitch oxidative-glycolytic fibers and presumably also motoneurons) demonstrates the tight correlation of the NADH-TR activity between these parts of the motor unit in both control and synergist-ablated muscles.
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PMID:Enzyme activity changes in rat soleus motoneurons and muscle after synergist ablation. 343 65

A light microscopy study on the localization of enzyme activity within atherosclerotic human intracranial arteries was performed on autopsy material obtained within 4 hours of death. The data suggests that the atherosclerotic process first goes through a proliferative phase and then a degenerative phase culminating in the formation of a plaque. In the proliferative phase, smooth muscle cell proliferation has formed a thickened intima. Tetrazolium reductase, adenosine triphosphatase (ATPase) and adenosine monophosphatase (AMPase) activities are present in these cells, while all dehydrogenases and acid phosphatase activities were weak or not present. As the degenerative phase commences, an area of necrosis, lipid and macrophage accumulation is formed on the lumen side of the elastica. This area increases in size until a plaque is formed. Unsaturated polar and nonpolar lipid, cholesterol, alpha-glycerophosphate dehydrogenase, acid phosphatase, and AMPase activities are associated with these areas and in foam cells, which are often found in the thickened intima of the proliferative phase. Tetrazolium reductase and ATPase activities decrease in the thickened intima as the area of necrosis increases in size, while dehydrogenase activity, except that for alpha-glycerophosphate, remains low or not present. Patterns of enzyme alterations for various stages of the disease process in intracranial arteries, the aorta and coronary arteries suggest a similar, if not identical, progression of the atherosclerotic process, irrespective of known differences in the prevalence of atherosclerosis.
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PMID:A histoenzymatic study of human intracranial atherosclerosis. 426 Jul 21

In order to relate the biogenesis of the lactose transport system to lipid synthesis, a glycerol-requiring mutant of Escherichia coli K-12 with a specific defect in l-glycerol-3-phosphate synthesis was isolated and characterized. The defective enzyme is the biosynthetic l-glycerol-3-phosphate dehydrogenase [l-glycerol-3-phosphate: NAD (P) oxidoreductase, EC 1.1.1.8] which functions as a dihydroxyacetone phosphate reductase to provide l-glycerol-3-phosphate for lipid synthesis. In this mutant, removal of glycerol from the growth medium results in inhibition of the synthesis of protein, deoxyribonucleic acid, and phospholipid. Inhibition of phospholipid synthesis immediately follows glycerol removal, whereas the inhibition of deoxyribonucleic acid and protein synthesis is preceded by a short lag period. Glycerol starvation does not change the turnover pattern of previously synthesized phospholipids. The blocking of lipid synthesis by glycerol starvation causes a drastic decrease in inducibility of beta-galactoside transport activity relative to beta-galactosidase, indicating that induction of lactose transport requires de novo lipid synthesis.
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PMID:Induction of the lactose transport system in a lipid-synthesis-defective mutant of Escherichia coli. 491 67

The activities of three enzymes--two mitochondrial and one microsomal--were measured in isolated islets of Langerhans from 2-month-old and 12-month-old rats. Mitochondrial glycerophosphate dehydrogenase activity (expressed as nanomoles of iodonitrotetrazolium reduced per minute per milligram of protein), decreased (P less than 0.01) from a mean (+/- SEM) of 73.2 +/- 11.2 (2-month-old) to 34.7 +/- 5.9 (12-month-old). In contrast, activities of neither mitochondrial monoamine oxidase nor microsomal NADH cytochrome-c reductase changed with age. These results demonstrate that the activity of the glycerophosphate shuttle decreases as rats grow older, and it raises the possibility that the consequent difficulty in regenerating cytosolic NAD+ may play a role in the insulin secretory defect associated with aging.
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PMID:Evidence of an age-related decline in mitochondrial glycerophosphate dehydrogenase activity of isolated rat islets. 635 35


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