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:1.6.5.2 (
NQO1
)
6,196
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
A major group of cholinergic neurons is present in the midbrain and pontine tegmentum. These cells could be selectively stained using either monoclonal antibodies to choline acetyltransferase, the pharmacohistochemical acetylcholinesterase procedure, or reduced
nicotinamide
adenine dinucleotide phosphate (NADPH)-
diaphorase
histochemistry. Using these three techniques, the precise distribution of this cell group was determined. By combining these techniques with immunohistochemical staining for various neuropeptides, examples of peptide-cholinergic coexistence could be demonstrated in this cell group. Approximately 30% of these cholinergic neurons displayed substance P immunoreactivity. Most of these cells also showed corticotropin-releasing factor immunoreactivity and bombesin/gastrin-releasing peptide immunoreactivity. These results therefore provide evidence for the coexistence of various neuropeptides together with NADPH-diaphorase activity in the ascending cholinergic reticular system.
...
PMID:Neuropeptides and NADPH-diaphorase activity in the ascending cholinergic reticular system of the rat. 396 Mar 9
Reduced
nicotinamide
adenine dinucleotide (NADH):ferricyanide reductase and
DT-diaphorase
specific activity in total homogenates of rat liver are markedly decreased as a very early biochemical event of hepatocarcinogenesis induced by the carcinogen 2-acetylaminofluorene (AAF). A 50 to 75% decrease in NADH:ferricyanide reductase was observed after 1 day of AAF (0.025% in the diet) feeding and persisted throughout a 7-week continuum of AAF administration. Carcinogen added directly to cell extracts had no effect. Similar results were obtained with single injections of either AAF or diethylnitrosamine. Xanthine dehydrogenase was also reduced in liver following AAF administration to nearly the same extent as NADH:ferricyanide reductase and
DT-diaphorase
. Total NADH-cytochrome c reductase and mitochondrial activity as estimated from succinic dehydrogenase were not affected by carcinogen administration relative to basal dietary controls. The reduced
nicotinamide
adenine dinucleotide phosphate:cytochrome c reductase that functions in drug detoxification was elevated. With livers of animals fed 4-acetamidophenol, a hepatotoxin chemically related to AAF, small decreases were noted in NADH:ferricyanide reductase, but not in xanthine dehydrogenase nor in
DT-diaphorase
. Initial lowering of these activities in the livers of the carcinogen-treated animals is preceded by or concomitant with a reduction in the levels of extramitochondrial pyridine nucleotides known from other studies to result from DNA damage.
...
PMID:Decreased NADH-oxidoreductase activities as an early response in rat liver to the carcinogen 2-acetylaminofluorene. 396 29
Rat liver postmitochondrial (S-12) fractions accounted for the bulk of the activity of whole cell homogenates in reducing chromium(VI) and accordingly in decreasing its mutagenicity. Both cytosolic (S-105) and microsomal fractions concurred to this process, which in all subcellular preparations tested was selectively induced by phenobarbital and especially by Aroclor 1254, but not by 3-methylcholanthrene. Cytosolic fractions were markedly more efficient in reducing chromium(VI) than microsomal fractions recovered from the same amount of tissue (liver or lung), although the latter preparations had a higher specific activity. The microsomal activity was exclusively NADPH dependent. A minor part of the cytosolic reduction was determined by nonenzymatic components, notably by some electron donors and chiefly by reduced glutathione, which proved to reduce chromium(VI) at physiological concentrations. However, also in cytosolic fractions, the most important contribution to chromium reduction was enzyme catalyzed, as shown by the following properties: thermolability; requirement for exogenous NADH or NADPH [supplied as such or in the form of a NADPH-generating system (S-9 mix)]; and saturation by chromium(VI). The likely involvement of
DT-diaphorase
in this metabolic process is supported by several findings, including its sharp pH dependence and its partial suppression by known inhibitors of this enzyme protein, such as p-chloromercuribenzoate, L-thyroxine, and dicumarol (which conversely did not counteract the metabolic deactivation of the other direct-acting mutagens 2-methoxy-6-chloro-9-[3-(2-chloroethyl)aminopropylamino]acridine 2HCl and epichlorohydrin). Similarly, cytosolic reduction of chromium(VI) was partially inhibited by selective metabolic depletors of both coenzymes of
DT-diaphorase
, i.e., NADPH and NADH. Pretreatment of rats with enzyme inducers (phenobarbital and 3-methylcholanthrene) stimulated the activity of
DT-diaphorase
in liver cytosolic fractions. A dramatic stimulation (35 to 40 times over untreated controls) was produced by Aroclor 1254, which also coinduced the liver cytosolic activity of enzymes involved in the glucose 6-phosphate-dependent pathway of both
nicotinamide
-adenine-dinucleotide phosphate and glutathione reduction (glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glutathione reductase). In the lung cytosol, a slight yet significant stimulation of some of these enzyme activities was determined by the daily intratracheal instillations of high doses of chromium(VI) itself for 4 weeks, a condition which has been found to enhance the pulmonary metabolism of this metal ion.
...
PMID:Prominent role of DT-diaphorase as a cellular mechanism reducing chromium(VI) and reverting its mutagenicity. 400 52
By means of the light and electron microscopy, histochemical and cytophotometrical methods the anterior subarea of the cerebral limbic cortex has been studied in 30 experimental and 30 control rabbits. The experimental animals have been given 3, 15 and 30 sessions (1 h per day) of electric irritation (0.05 mA, 50 Hz, 1 msec) on the posterior hypothalamic field (PHF). Twelve rabbits from 30 control animals make an intact group and 18--a group with inactive electrodes inserted into the PHF. After 3 and especially after 15 sessions it has been revealed: in neurons--an acute swelling, edematous alterations, hyperchromatosis and shrinkage, changes in lactate dehydrogenase, succinic dehydrogenase,
nicotinamide
-adenine-dinucleotide-
diaphorase
and
nicotinamide
-adenine-dinucleotide-phosphate-
diaphorase
activities, in neuroglia--hypertrophy and weakly manifested hyperplasia. After 30 sessions synapses degenerated after the dark type are revealed. More intensive structural and metabolic changes are noted in the middle cytoarchitectonical complex. The changes of the enzymatic activity are considered as certain signs of weakening mitochondrial processes, connected with energy production, increasing glycolysis, decreasing level of the energetic provision of the cytoplasmic synthesis, arising under conditions of a disturbed transneuronal influence on the cortex by the hypothalamus.
...
PMID:[Structural and metabolic changes in the limbic cortex of the rabbit in response to experimentation with the hypothalamus]. 408 71
Previous papers in the series have shown that the surface membranes of herpesvirus-infected cells acquire new immunological specificities and that purified infected cell membrane preparations, characterized by their physical properties rather than topology in the cell, contain new glycoproteins genetically determined by the virus. In this study, we prepared purified plasma membrane identified by its 5' nucleotidase, fucose, and reduced
nicotinamide
adenine dinucleotide-
diaphorase
content. Analysis of the membrane proteins and glycoproteins by electrophoresis in acrylamide gels indicated the following. (i) Purified plasma membranes from infected cells contained two sets of proteins, i.e., host proteins were present both before and after infection and viral proteins were present only after infection. (ii) After infection, no appreciable selective or nonselective loss of host proteins from membranes was demonstrable. However, no new host proteins were made. (iii) Electropherograms of plasma membrane proteins from infected cells indicated the presence of at least 12 virus-specific proteins ranging in molecular weight from 25 x 10(3) to 126 x 10(3) daltons. Of these, at least nine were glycosylated. Proteins and glycoproteins with similar electrophoretic mobilities but in somewhat different ratios were also present in preparations of highly purified virions.
...
PMID:Proteins specified by herpes simplex virus. VI. Viral proteins in the plasma membrane. 411 36
Total reduced
nicotinamide
adenine dinucleotide (NADH) and reduced
nicotinamide
adenine dinucleotide phosphate (NADPH)
diaphorase
activities were examined in human neutrophils. Approximately two-thirds of each enzyme activity was located in the granule fraction with the remainder in the soluble. The activities in a 27,000 x g supernatant from a sonic extract of human polymorphonuclear leukocytes were characterized. Both NADH and NADPH diaphorase were insensitive to cyanide and azide and showed greater activity at acid pH. K(m) values for nitroblue tetrazolium were not markedly different (33 muM with NADH and 12 muM with NADPH), but there was a 40-fold difference in K(m) for the reduced pyridine nucleotides (10 muM with NADH and 400 muM for NADPH). Since the intracellular concentration of both nucleotides is estimated to be about 50 muM, it is much more likely, from a kinetic argument, that the respiratory burst of phagocytosis is intiated by the oxidation of NADH rather than of NADPH.
...
PMID:Reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate diaphorase activity in human polymorphonuclear leukocytes. 415 6
The cytochemical localization, by conventional methods, of lactate and glyceraldehyde-3-phosphate dehydrogenases is limited, firstly, by the solubility of these enzymes in aqueous media and, secondly, by the dependence of the final electron flow from reduced
nicotinamide
-adenine dinucleotide (NADH) to the tetrazolium on tissue
diaphorase
activity: localization is therefore that of the
diaphorase
, which in rabbit adductor magnus is mitochondrial. NADH has been found to have great affinity to bind in the sarcoplasmic reticulum, and, therefore, if it is generated freely in the incubation media containing 2,2',5,5'-tetra-p-nitrophenyl-3,3'-(3,3'-dimethoxy-4,4'-phenylene)-ditetrazolium chloride (TNBT) and N-methyl phenazonium methyl sulfate (PMS), it can bind there and cause a false staining. Since such a production of NADH can readily occur in the incubation media for glycolytic dehydrogenases due to diffusion of these soluble enzymes from tissue sections, the prevention of enzyme solubilization is extremely important. Fixation in formaldehyde prevented such enzyme diffusion, while at the same time sufficient activity persisted to allow for adequate staining. The incubation media contained PMS, so that the staining system was largely independent of tissue
diaphorase
activity. Application of these methods to adductor magnus of rabbit revealed by light microscopy, for both enzymes, a fine network which was shown by electron microscopy to represent staining of the sarcoplasmic reticulum. Mitochondria also reacted. These findings add further support for the notion that the sarcoplasmic reticulum is probably involved in glycolytic activity.
...
PMID:Cytochemical localization of two glycolytic dehydrogenases in white skeletal muscle. 428 29
Isolated membranes of Bacillus stearothermophilus 2184D can be disrupted by treatment with sodium dodecyl sulfate (SDS). This disruption is attended by a decreased turbidity of membrane suspensions and a differential loss of activities of the electron transport system. Reduced methyl viologen (MVH)-nitrate reductase activity is insensitive to SDS treatment, whereas reduced
nicotinamide
adenine dinucleotide (NADH)-nitrate reductase and cyanide-sensitive NADH oxidase activities are decreased by 80% at an SDS concentration of 0.5 mg/mg of membrane protein.
NADH-menadione reductase
activity is unaffected at this SDS concentration, but at higher detergent levels it also decreases in activity. The abilities of NADH to reduce and nitrate to oxidize the cytochrome components of the membrane were also decreased after SDS treatment. Dilution of solubilized membrane in buffer containing divalent cation results in formation of an aggregate with an increased turbidity and reconstituted NADH-nitrate reductase and cyanide-sensitive NADH oxidase activities. Of several cations tested, magnesium was the most effective, and the reconstitution process was pH-dependent with an optimum at pH 7.4. Intact and aggregated membranes had similar densities and cytochrome contents, and the sensitivity of NADH-nitrate reductase to several inhibitors was similar in intact and reconstituted membranes.
...
PMID:Physical aggregation and functional reconstitution of solubilized membranes of Bacillus stearothermophilus. 433 10
Optochin-resistant mutant and wild-type diaphorases were purified approximately 300-fold by a combination of batch adsorption and column chromatography with diethylaminoethyl cellulose, and were characterized with regard to their pH optima, sensitivity to optochin inhibition and heat inactivation, Michaelis constants with flavine mononucleotide (FMN) and reduced
nicotinamide
adenine dinucleotide (NADH), and inhibition constants with optochin hydrochloride. The pH optima of the purified diaphorases were similar, but the purified diaphorases from the optochin-resistant strains were approximately four to five times more resistant to heat inactivation at 45 C than was the wild-type
diaphorase
. Purified
diaphorase
preparations from the optochin-resistant pneumococci had greater activities per milligram of protein and were more resistant to optochin inhibition than the preparation from the optochin-sensitive pneumococcus. Michaelis constants for FMN and NADH were similar; however, the inhibition constants of the optochin-resistant diaphorases were four to eight times greater than that of the optochin-sensitive
diaphorase
. Optochin hydrochloride produced a noncompetitive type of inhibition with FMN as substrate but a competitive type of inhibition with NADH as substrate. Optochin hydrochloride produced an approximately 10-fold increase in the Michaelis constant for NADH. The concentration of drug required to produce this effect was, however, greater with the mutant diaphorases than with the wild-type
diaphorase
. Optochin hydrochloride quenched the fluorescence of riboflavine. This phenomenon did not appear to be related to the
diaphorase
-inhibitory activity of the drug, however, since the pH requirements of the two reactions were different. Quenching of riboflavine fluorescence by optochin hydrochloride increased with a rise in pH, whereas inhibition of
diaphorase
activity by optochin hydrochloride was greater at pH 6.8 than at pH 7.6.
...
PMID:Purification and properties of mutant and wild-type diaphorases from Diplococcus pneumoniae. 438 90
Evidence that the bactericidal ability and the stimulated oxidative metabolism of leukocytes appear in parallel during fetal development of the Minnesota Miniature pig has been obtained by application of the techniques applied to studies of human cells. It was demonstrated that leukocytes from 87- to 90-day fetuses were fully capable of ingesting Staphylococcus aureus but greatly diminished in bactericidal capacity as compared to leukocytes of older fetuses and adults. Although resting levels of oxygen consumption and hexose monophosphate pathway activity of leukocytes from the younger fetuses compared well with those of leukocytes from older animals, the phagocytosis-stimulated increments of metabolism were much less at 87 to 90 days of gestation than at later developmental stages. Both bactericidal capacity and increased metabolism of leukocytes reach adult levels by 100 days of gestation (normal gestation period of 115 to 120 days). Acrylamide gels stained for reduced
nicotinamide
adenine dinucleotide (NADH) and NADH phosphate (NADPH)
diaphorase
activity after disc electrophoresis of leukocyte extracts revealed normal mobility and intensity of NADH diaphorase bands. Three NADPH diaphorase bands were present in adult leukocyte extracts. Only the fast-migrating NADPH diaphorase band of 87- to 90-day cells stained with decreased intensity. This "deficiency" was no longer present at the later fetal period. The fast-migrating NADPH diaphorase band may represent an electron transfer protein which functions in cyanide-insensitive respiration of the leukocytes of the pig.
...
PMID:Development of bactericidal capacity and phagocytosis-associated metabolism of fetal pig leukocytes. 463
<< Previous
1
2
3
4
5
6
7
8
9
10