Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:1.8.1.4 (diaphorase)
2,754 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The method of visual quantitative estimation was employed to determine the index of enzymes activity in embryonal cells cultures infected with Rous virus. In early terms (1-7 days after infection) a moderate production of diformazane was noted in the presence of glucoso-6-phosphatiosomerase, phosphoglucomutase, pyruvatoxidase, NAD. H2- and NADP. H-2-diaphorase, other enzymes showing no distinquishable deviations in the activity, as compared with the normal culture. In later terms (13-27 days) during the proliferation of the transformed cells there was found an increased level of the glycolysis enzymes activity, pentose cycle, hydrolysis of ortho-phosphoric acid monoethers and reduced lemon acid cycle and tissue respiration. Cytoplasmatic vacuoles formed in the transformed cells seem to represent hypertrophic lysosomes and phagolysosomes.
...
PMID:[Quantitative cytochemical detection of enzymes in cultured cells following infection with Rous virus]. 17 56

Experiments were conducted on rabbits. A study was made of the activity of the redox enzymes--glucose-6-phosphate dehydrogenase (G-6-PDH), lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NAD-and NADP-diaphorases, cytochromeoxidase (CCO), alpha-glycerophosphate dehydrogenase (alpha-GPDH) in the supraoptic and paraventricular nuclei of the hypothalamus and the posterior lobe of the hypophysis under conditions of stimulation and removal of the superior cervical sympathetic ganglia. There was revealed a correlation between the activity of the tissue respiration enzymes (SDH, MDH, NAD- and NADP-diaphorase, CCO) and the functional condition of the hypothalamo-neurohypophysial neurosecretory system. However, the enzymes of the pentose-phosphate (G-6-PDH) and glycerophosphate shunt (alpha-GPDH) and also of the anaerobic way of oxidation (LDH) reacted nonspecifically on the induced effects.
...
PMID:[Effect of removal and stimulation of the superior cervical sympathetic ganglia on the activity of oxidation-reduction enzymes in the neurosecretory cells of the anterior hypothalamus in rabbits]. 20 40

The authors have studied the enzymhistochemical and ultrastructural pictures of tenocytes of adult human tendons. High succinate dehydrogenase, cytochrome oxidase, TPN-diaphorase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity were found, as indicated both oxidativ, anaerobic and pentose-phosphate shung activity. Phosphorylase and glutamate dehydrogenase activity was medial, lipase and alcaline phosphatase activity was slight. In tenocytes well developed rough endoplasmic reticulum and GOLGI apparatus, large amount of free ribosomes were found.
...
PMID:Histochemical and ultrastructural study of adult human tendon. 23 84

Quantitative cytochemical techniques have been employed in a study of some of the acute effects of low doses (0.01----1 mU/liter) of TSH on the metabolism of guinea pig thyroid segments maintained in nonproliferative organ culture. The enzymes involved in the synthesis of NADP+ (NAD+ kinase), its reduction by the pentose-shunt (glucose 6-phosphate dehydrogenase), and its reoxidation both by the microsomal electron chain (diaphorase activity) and by participation in other cellular processes, have been examined. The effect of TSH on peroxidase activity has also been studied. After 10 min stimulation with TSH (1 mU/liter) there was a 60% increase in NAD+ kinase activity which preceded changes in the microsomal reoxidation of NADPH (up 33% by 30 min). There were no changes in the activity of glucose 6-phosphate dehydrogenase. There was a sustained rise in peroxidase activity which reached 129% over control after 30 min. This is the first in vitro demonstration of an acute stimulation of peroxidase and kinase activities by physiological concentrations of TSH. NADPH reoxidation after stimulation with TSH was such that the ratio of NADPH reoxidized via the microsomal respiratory pathway (diaphorase, hydrogen pathway 1) relative to that available for cytosolic utilization (hydrogen pathway 2) increased compared to the unstimulated controls. We suggest that increased NADP+ production (via NAD+ kinase activity) and the preferential shuttling of the NADPH for reoxidation via the microsomal respiratory pathway, coupled with greatly stimulated peroxidase activity, may be important regulators of the control of thyroglobulin iodination and hence thyroid hormone production.
...
PMID:Acute stimulation of thyroidal NAD+ kinase, NADPH reoxidation, and peroxidase activities by physiological concentrations of thyroid stimulating hormone acting in vitro: a quantitative cytochemical study. 284 14

Quantitative histochemical assays of several enzymes (succinic, lactic, beta-hydroxybutyrate, alpha-glycerophosphate, and glucose-6-phosphate dehydrogenases, NAD diaphorase, and phosphorylase) in the myocardium of persons who had died suddenly with postinfarctional cardiosclerosis have failed to reveal any changes specific for this patient group. Direct correlations were established between the enzyme activities assayed, on the one hand, and the extent of myocardial hypertrophy and the signs of chronic heart failure, on the other. The activities of beta-hydroxybutyrate dehydrogenase and glucose-6-phosphate dehydrogenase, which are involved in fatty acid utilization and in the pentose phosphate pathway, were elevated in cases of moderate hypertrophy, as were those of all redox enzymes in cases of strongly marked hypertrophy, although they were reduced in cases with signs of chronic cardiac failure despite the presence of considerable myocardial hypertrophy. Areas of acute myocardial ischemia were discovered in 45% of the cases.
...
PMID:[Histochemical study of the enzyme activity of the myocardium of sudden death victims with postinfarct cardiosclerosis]. 296 Feb 98

Osteogenesis of the body of the mandible in embryonic and neonatal rats was studied histologically and by histochemistry to determine the role of Meckel's cartilage in bone formation. Meckel's cartilage showed intense activity of lactate dehydrogenase and NADH2-diaphorase and weak activity of acid phosphatase, indicating a functioning citric acid cycle, pentose phosphate shunt and a capacity for anaerobic metabolism. The activity of these enzymes declined after hypertrophy of Meckel's cartilage. Alkaline phosphatase was the major enzyme of mineralising mandibular osteoid and was present in the osteoblasts and osteoprogenitor cells but not in Meckel's cartilage. After the differentiation of Meckel's cartilage and intramembranous bone, Meckel's cartilage supported mandibular bone formation by endochondral ossification in the anterior part of the mandible.
...
PMID:Enzyme histochemical analysis of Meckel's cartilage. 325 49

Pathological alterations of chronic Achilles paratenonitis were studied histologically and histochemically in tissue samples obtained operatively from 16 athletes with this complaint and from 3 control patients. The activities of 11 different enzymes--lactate, succinate, malate, glucose-6-phosphate and glutamate dehydrogenases, lipoamide dehydrogenase and glutathione reductase (NADH2- and NADPH2-diaphorases), acid and alkaline phosphatases, phosphorylase and leucylaminopeptidase--were studied. Pathological findings were located diffusely around the tendon. A slight inflammatory cell reaction was found in all cases. The fatty areolar tissue was clearly thickened and edematous, and showed fibrinous exudations, widespread fat necrosis, considerable connective tissue proliferation and adhesion formation. The blood vessels showed profound degenerative and necrotizing changes. The thin membranes of the paratenon were clearly hypertrophied. Increased enzyme activities were mainly found in the fibroblasts, inflammatory cells and vascular walls. A moderate activity of lysosomal enzymes, an increased activity of enzymes of electron transport, anaerobic glycolysis, pentose phosphate shunt and decreased activity of those of aerobic energy metabolism were found. Simultaneously an increased amount of both neutral and acid mucopolysaccharides and a locally increased amount of elastic fibres were found in the inflamed paratenon. These results indicate that marked metabolic changes occur in paratenonitis, i.e. an increased catabolism and decreased oxygenation of the inflamed areas. The morphological alterations suggest that the gliding function of the paratenon may be impaired.
...
PMID:Chronic Achilles paratenonitis in athletes: a histological and histochemical study. 358 19

Oxygen and glucose consumption and lactate production of the peritoneal membrane and intra-abdominal adhesions were measured in rats after a single intra-peritoneal colloidal silica injection. Enzyme histochemical studies were made of lactate dehydrogenase, succinate dehydrogenase, NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, acid phosphatase, leucylaminopeptidase and alkaline phosphatase in the peritoneal membrane. Anaerobic glycolysis comprises 47% of the total glucose consumption in the the normal peritoneum. Glucose consumption and lactate production of the peritoneal membrane increased sharply in the early phase of silica-induced peritonitis and stayed at a high level for a week indicating an enhanced anerobic metabolism. Oxygen and aerobic glucose consumption increased more slowly than anaerobic glucose consumption and reached their maxima 1 week after silica injection, indicating that the rate of aerobic metabolism is also higher in chemical peritonitis than in the controls. On the other hand, glucose consumption and lactate production increased in a parallel fashion in adhesions and in the peritoneum in the early phase of peritonitis. However, the maximum and later levels were less in adhesions than in the peritoneum. In the enzyme histochemical study high activities of enzymes indicating anaerobic energy metabolism and metabolism via the pentose phosphate shunt were seen in cells of the peritoneal membrane during the early phase of peritonitis. No activity was identified in enzymes indicating aerobic energy metabolism and increased catabolism before the end of the first week.
...
PMID:Energy metabolism of the peritoneal membrane in silica-induced peritonitis. A biochemical and enzyme histochemical study. 625 64

The lipoamide dehydrogenase (LPD) encoded by lpdA gene is a component of the pyruvate dehydrogenase complex (PDHc), alpha-ketoglutarate dehydrogenase (AKGDH) and the glycine cleavage multi-enzyme (GCV) systems. In the present study, cell growth characteristics, enzyme activities and intracellular metabolite concentrations were compared between the parent strain Escherichia coli BW25113 and its lpdA knockout mutant in batch and continuous cultures. The lpdA knockout mutant produced significantly more pyruvate and L-glutamate under aerobiosis. Some D-lactate and succinate also accumulated in the culture broth. Based on the investigation of enzyme activities and intracellular metabolite concentrations, acetyl-CoA was considered to be formed by the combined reactions through pyruvate oxidase (PoxB), acetyl-CoA synthetase (Acs) and acetate kinase (Ack)-phosphoacetyltransferase (Pta) in the lpdA mutant. The effect of the lpdA gene knockout on the intracellular metabolic flux distributions was investigated based on 1H-13C NMR spectra and GC-MS signals obtained from 13C-labeling experiment using the mixture of [U-13C] glucose, [1-13C] glucose, and naturally labeled glucose. Flux analysis of the lpdA mutant indicated that the Entner-Doudoroff (ED) pathway and the glyoxylate shunt were activated. The fluxes through glycolysis and oxidative pentose phosphate (PP) pathway (except for the flux through glucose-6-phosphate dehydrogenase) were slightly downregulated. The TCA cycle was also downregulated in the mutant strain. On the other hand, the fluxes through the anaplerotic reactions of PEP carboxylase, PEP carboxykinase and malic enzyme were upregulated, which were consistent with the results of enzyme activities. Furthermore, the influence of the poxB gene knockout on the growth of E. coli was also studied because of its similar function to PDHc which connects the glycolysis to the TCA cycle. Under aerobiosis, a comparison of lpdA mutant and poxB mutant indicated that PDHc is the main enzyme which catalyzes the reaction from pyruvate to acetyl-CoA in the parent strain, while PoxB plays a very important role in the PDHc-deficient strain.
...
PMID:Effect of lpdA gene knockout on the metabolism in Escherichia coli based on enzyme activities, intracellular metabolite concentrations and metabolic flux analysis by 13C-labeling experiments. 1631 Feb 73

Lactobacillus is a probiotic commonly used for supplementation to human and animal diets. In this study, we used 2-DE and MS to analyze changes in the proteomes of Lactobacillus and intestinal epithelial cells in two model systems. The in vivo and in vitro models were involved the inoculation of Lactobacillus fermentum I5007 into the rabbit jejunum for 4 h and the culture of the bacterium with Caco-2 cells for 1 h, respectively. Our results indicate that, after exposure to the intestinal environment, the bacterium exhibited decreases in key enzymes involved in energy metabolism (e.g., lactate dehydrogenase, dihydrolipoamide dehydrogenase, and nicotinate phosphoribosyltransferase) and amino acid metabolism (e.g., arginyl-tRNA synthetase and aspartate-semialdehyde dehydrogenase), but increases in glycoside hydrolase (an enzyme for mucin degradation) and fructose-6-phosphate phosphoketolase (an enzyme of the pentose phosphate pathway). In response to an interaction with L. fermentum I5007, Caco-2 cells showed changes in proteins that were beneficial for gut integrity, including voltage-dependent anion channel 1, glutathione transferase, and heat shock protein gp96. On the basis of their functions, we suggest that these proteins serve as useful biomarkers for metabolic changes in Lactobacillus and intestinal epithelial cells in response to their interactions.
...
PMID:2-DE and MS analysis of interactions between Lactobacillus fermentum I5007 and intestinal epithelial cells. 1800 11


1 2 Next >>

---