Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.1 (NADPH-diaphorase)
 3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Female albino rats were treated with a total of 28 mg of chlormadinone acetate (CMA) for 28 days. In the adrenal cortex, the ovary, the vagina, and the uterus the activities of 3-beta-ol-steroiddehydrogenase, of dl-beta-OH-butric acid dehydrogenase, of alcaline and acid phosphatases, of DPN-diaphorase, of ATP-ase, and of non-specific esterases do not differ from untreated controls. 2. In the external muscle layer of the myometrium strong cholinesterase (ChE) activity was induced by C.M.A. A corresponding high ChE activity is normally found in immature rats or in estrus. 3. Furthermore, by treatment with CMA, ChE activity was induced in the tubular glands of the endometrium. This activity is found in the small parts of glomerate glandular terminals only but not in the rest of the glandular epithelium, nor in the epithelium of the cavum. It could be demonstrated that a corresponding ChE activity normally appears in the second third of pregnancy. The ChE activity induced by CMA was considerably higher and more widespread than during normal pregnancy. 4. It is concluded that in the endometrial glands a development similar to pregnancy is initiated by CMA. But development stops at the stage of ChE activity, thus leading to accumulation of ChE active cells.
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PMID:[Enzyme histochemical studies on the rat adrenal cortex, ovary, uterus and vagina following chlormadinone acetate administration, especially cholinesterase activity in myometrium and endometrium]. 5 Feb 31

Muscle fiber composition and oxidative and glycolytic enzymatic activity have been studied with complete traumatic transection of the spinal cord and spastic paralysis of the lower extremities. Muscle sample were taken by means of needle biopsy from the vastus lateralis, gastrocnemius, and soleus muscles. Biopsies were also taken for comparison from the deltoid muscle. Fibers staining darkly for alkaline stable myofibrillar ATP-ase (type II) dominated or were the only fibers identified in the paralysed muscles. The deltoid muscles of the same patients had a rather even mixture of type I and II fibers. Staining pattern was reversed after acid preincubation (pH 4.3). Mean diameters in the paralysed muscles were reduced for both fiber types. All fibers stained relatively weakly for NADH-diaphorase. Succinyldehydrogenase activity was low and phosphofructokinase activity usually moderately reduced. The findings imply that neuronal influence on the muscular fibers had led to a change in the staining characteristics of the muscle fibers. Such a change migh indicate altered contractile characteristics, though the detailed nature of the observed findings in still unclear.
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PMID:Muscle fiber composition in patients with traumatic cord lesion. 13

Biopsies from vastus lateralis muscle of male patients suffering from chronic ethanol abuse were studied with regard to histochemical reactions of ATPase and NADH-diaphorase; enzymatic activities of triosephosphate dehydrogenase (TPD), lactate dehydrogenase (LD), and cytochrome c oxidase (cytox); content of ATP, creatine phosphate, and glycogen; and volume fractions of fat, mitochondria, and fibrillar and extrafibrillar space. The results were compared with those from controls without known abuse of ethanol. The relative numbers of fibers were the same in two groups, but the size of the fast-twitch-glycolytic (white) fibers was diminished in the alcoholic group. The activities of TPD and LD were diminished in skeletal muscle of the alcoholics. This is most probably caused by the reduced amount of fast-twitch-glycolytic tissue, as there was a good correlation between this amount and the activity of the two enzymes. The activity of cytox was slightly lower in muscle of the alcoholics than in that of the controls. The volume fraction of mitochondria was lower in the alcoholic group than in the control group. Volume fractions of fat and fibrillar and extrafibrillar space were equal in the two groups. No significant differences were found in the amount of glycogen and ATP in the muscle of the two groups. However, the content of creatine phosphate is higher in the alcoholic group than in the control group.
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PMID:Effects of chronic ethanol abuse on structure and enzyme activities of skeletal muscle in man. 17 13

The protective action of aspartic acid on isolated and perfused rat liver was studied. In case of D-galactosamine intoxication the GOT, GPT and SDH activity and the lactate and pyruvate concentration in the perfusion medium were less augmented and the glycogen level in hepatic tissue was less diminished in animals treated with aspartic acid, as compared to controls. The histochemical applied (PAS reaction for glycogen, nucleic acids, NADH2-diaphorase, glucose-6-phosphatase and membrane-ATP-ase), also stated a protecting effect in the treated animals. The protective action of aspartate is hypothetically considered to be exerted by its capacity to reestablish the cellular deficit of pyridine nucleotides and thus to improve the synthesis of nucleic acids, glycoprotein and glycolipids or/and by its participation in various metabolic pathways.
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PMID:Protecting action of aspartate on the hepatic changes induced by D-galactosamine. 18 87

The organic phosphate allosteric effectors of hemoglobin, inositol hexaphosphate, 2,3-diphosphoglycerate, and ATP, interact with NADH-methemoglobin reductase (NADH-diaphorase). Significant inhibitory effects on the enzyme were found when dichlorophenolindophenol, or ferricyanide were used as electron acceptors in place of methemoglobin. In contrast, apparent stimulation of enzyme activity was observed when adult human methemoglobin was used as the electroganic phosphate on the rate of reaction due to its interaction with the substrate methemoglobin to produce the favored T type of quaternary conformation. The inhibitory effect of inositol hexaphosphate on the enzyme is associated with a perturbation in the reactivity of essential sulfhydryl group(s) on the enzyme. It is suggested that the interaction of the organic phosphate with the enzyme as well as with the substrate is significant in determining the overall rate of methemoglobin reduction.
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PMID:Inhibition of NADH-methemoglobin reductase by organic phosphates. 49 34

Aminooxyacetic acid (AOAA) is an inhibitor of several pyridoxal phosphate-depedent enzymes in the brain. In the present experiments intrastriatal injections of AOAA produced dose-dependent excitotoxic lesions. The lesions were dependent on a pyridoxal phosphate mechanisms because pyridoxine blocked them. The lesions were blocked by the noncompetitive N-methyl-D-aspartate (NMDA) antagonist MK-801 and by coinjection of kynurenate, a result indicating an NMDA receptor-mediated excitotoxic process. Electrophysiologic studies showed that AOAA does not directly activate ligand-gated ion channels in cultured cortical or striatal neurons. Pentobarbital anesthesia attenuated the lesions. AOAA injections resulted in significant increases in lactate content and depletions of ATP levels. AOAA striatal lesions closely resemble Huntington's disease both neurochemically and histologically because they show striking sparing of NADPH-diaphorase and large neurons within the lesioned area. AOAA produces excitotoxic lesions by a novel indirect mechanism, which appears to be due to impairment of intracellular energy metabolism, secondary to its ability to block the mitochondrial malate-aspartate shunt. These results raise the possibility that a regional impairment of intracellular energy metabolism may secondarily result in excitotoxic neuronal death in chronic neurodegenerative illnesses, such as Huntington's disease.
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PMID:Aminooxyacetic acid results in excitotoxin lesions by a novel indirect mechanism. 183 Jun 13

The NADPH dehydrogenase of the cyanobacterium Anabaena variabilis was solubilized, purified, and characterized. Activity staining after nondenaturing polyacrylamide gel electrophoresis, kinetics, and immunological characterization led to the conclusion that only one thylakoid-associated NADPH dehydrogenase exists in Anabaena, identical with ferredoxin-NADP+ oxidoreductase (FNR). After sodium dodecyl sulfate-polyacrylamide gel electrophoresis an intense band at 34 kDa and a weak band at 52 kDa were found by immunoblotting with an antibody against Anabaena FNR. Using a cell-free preparation competent of oxidative phosphorylation it was demonstrated that FNR operates as a respiratory NADPH dehydrogenase coupled to cyanide-sensitive oxidative ATP formation.
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PMID:Ferredoxin-NADP+ oxidoreductase is the respiratory NADPH dehydrogenase of the cyanobacterium Anabaena variabilis. 246 78

Wistar rats (110-125 g) were irradiated with a single dose of 500 R. Histochemical studies were done concerning the glycoproteins (GP) of sublingual glands, gastric, small intestine and colon mucosa, and some intestinal enzymes: acid and alkaline phosphatase (ACP, ALP) leucineaminopeptidase (LAP), Mg-dependent ATP-ase, NADH-diaphorase, lactic dehydrogenase (LDH). After irradiation all these reactions were diminished, with a maximal effect between 3-5 days. This impairment is in accord with the maximal lethality in this interval after such a degree of irradiation that produced the gastrointestinal syndrome. Cocarboxylase, a radioprotector, improved these changes regarding the structures of the small intestine and also the GP of sublingual glands, stomach, small intestine and colon, demonstrating there its efficiency.
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PMID:Histochemical changes in the digestive tract in irradiated rats. 311 66

The individual effects of two putative metabolites of primaquine (5,6-dihydroxyprimaquine and 5,6-dihydroxy-8-aminoquinoline) on the hexose monophosphate shunt (HMS) and on the ATP-dependent proteolytic system which rapidly degrades oxidized erythrocyte protein were measured in intact red blood cells in vitro from two blood donors. In red cells treated with nitrite (1-40 mM) or phenylhydrazine (0.01-10 mM), proteolytic activity was detected only with concentrations (7.5 mM NaNO2 and 0.25 mM phenylhydrazine) causing greater than 15-fold elevation of HMS activity, and glucose-6-phosphate dehydrogenase (G6PD)-deficient (25% of normal activity) red cell suspensions thus treated showed approximately 30% greater proteolysis. G6PD-normal and deficient red cells treated with the primaquine analogs, however, did not experience proteolysis with concentrations (0.25 mM) in excess of those causing 17-fold elevation of HMS activity. Stimulation of the HMS by the primaquine analogs thus appears unrelated to an erythrotoxic oxidative stress. Methylene blue is known to cause an elevation of HMS activity through direct and diaphorase II-dependent oxidation of reduced nicotinamide adenine dinucleotide phosphate (NADPH) which is independent of injurious oxidative stress. It was found that the putative primaquine metabolites also caused direct and diaphorase II-dependent oxidation of NADPH in dilute hemolysate, thus suggesting that the putative primaquine metabolites have a methylene blue-like redox disposition in red blood cells. Results obtained in this study suggest that the hemolytic toxicity of primaquine may be unrelated to processes which lead to oxidative deterioration of red cell protein.
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PMID:Oxidative activity of hydroxylated primaquine analogs. Non-toxicity to glucose-6-phosphate dehydrogenase-deficient human red blood cells in vitro. 375 45

A histochemical study of the metabolism of rat renal arteries and arterioles. Rat renal arteries and arterioles were examined histochemically to determine their metabolic profiles. Succinate, malate and NAD-isocitrate dehydrogenase, cytochrome oxidase and ubiquinone were assessed to determine aerobic metabolism. Glucose-6-phosphate dehydrogenase and DPN diaphorase were evaluated to determine hexose-monophosphate-shunt activity. Anaerobic metabolism was evaluated via lactate dehydrogenase, and the substrate, glycogen. Gomori's lipase, beta-hydroxybutyrate dehydrogenase and amounts of neutral fat and free fatty acids were assessed as indicators of lipid utilization. Myosin ATPase activity was evaluated as an index of ATP utilization for contraction. Deoxyribonucleic and ribonucleic acids were appraised as indicators of protein synthesis. In general, the oxidative enzymes and myosin ATPase demonstrate considerable activity in renal arteries and arterioles which suggests aerobic metabolism and ATP usage. Renal arteries and arterioles also appear capable of anaerobic metabolism as indicated by strong lactate dehydrogenase reactivity and by the presence of slight to moderate quantities of glycogen, while high levels of glucose-6-phosphate dehydrogenase and moderate amounts of deoxyribonucleic acid suggest a potential for beta-hydroxybutyrate dehydrogenase, minimal lipase activity, and the absence of fatty acids with substantial amounts of neutral fat, indicate limited lipid catabolism.
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PMID:A histochemical study of the metabolism of rat renal arteries and arterioles. 620 11


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