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

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Query: EC:1.6.99.1 (NADPH-diaphorase)
3,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The substantia innominata encompasses an area of the basal forebrain that is ventral to the lenticular nucleus and anterior commissure, medial to the claustrum and external capsule, and lateral to the hypothalamus. The nucleus basalis of Meynert consists primarily of large acetylcholinesterase (AchE)-positive neurons embedded within the substantia innominata. Damage to these neurons may be important in the pathogenesis of cortical dysfunction in Alzheimer's disease. In order to characterize other neuronal elements in the substantia innominata and their relationship to the nucleus basalis, we chose to study a biochemically distinct neuronal subset containing the enzyme nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d). The substantia innominata was blocked from six normal brains obtained postmortem and fixed in neutral-buffered formalin at 4 degrees C for 48 hours. Free-floating 50-micron sections from several levels were stained for NADPH-d or AchE activities. Selected sections were double stained for NADPH-d and AchE. NADPH-d activity was present in a network of pleomorphic neurons that extended through all levels of the substantia innominata and into the striatum and amygdala. NADPH-d neurons were particularly numerous at the level of the anterior commisure and were closely associated with the cholinergic neurons of the nucleus basalis. They were not seen in the ventral pallidum, or the vertical limb of the diagonal band of Broca or in the islands of Calleja. The cell bodies of NADPH-d neurons were quite varied in shape, ranging from ovoid to fusiform, and about half the cells were bipolar. Where neuronal density was high, their dendrites formed an interlacing pattern. NADPH-d-positive fibres were seen coursing through the external capsule, hypothalamus, and amygdala. This novel set of neurons in the substantia innominata may be part of a more extensive network that interacts with the magnocellular basal forebrain system at the level of the nucleus basalis. Whether other neurotransmitters are present within these neurons and whether NADPH-d neurons are involved in Alzheimer's disease remain to be elucidated.
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PMID:Subset of neurons characterized by the presence of NADPH-diaphorase in human substantia innominata. 361 5

This work tested whether the membrane electrical properties of cat motoneurons, the contractile properties of their muscle units, and the normal relationships among them would be restored 9 mo after section and resuture of their muscle nerve. Properties of medial gastrocnemius (MG) motor units were examined 9 mo following section and resuture of the MG nerve in adult cats. Motoneuron electrical properties and muscle-unit contractile properties were measured. Motor units were classified on the basis of their contractile properties as type fast twitch, fast fatiguing (FF), fast twitch with intermediate fatigue resistance (FI), fast twitch, fatigue resistant (FR), or slow twitch, fatigue resistant (S) (8, 20). Muscle fibers were classified as type fast glycolytic (FG), fast oxidative glycolytic (FOG), or slow oxidative (SO) on the basis of histochemical staining for myosin adenosine triphosphatase, nicotinamide adenine dinucleotide diaphorase, and alpha-glycerophosphate dehydrogenase (48). Following 9 mo self-reinnervation, the proportions of each motor-unit type were the same as in normal control animals. Motoneuron membrane electrical properties [axonal conduction velocity, afterhyperpolarization (AHP) half-decay time, rheobase, and input resistance] also returned to control levels in those motoneurons that made functional reconnection with the muscle (as determined by ability to elicit measurable tension). The relationships among motoneuron electrical properties were normal in motoneurons making functional reconnection. Approximately 10% of MG motoneurons sampled did not elicit muscle contraction. These cells' membrane electrical properties were different from those that did elicit muscle contraction. Contractile speed and fatigue resistance of reinnervated muscle units had recovered to control levels at 9 mo postoperation. Force generation did not recover fully in type-FF units. The reduced tensions were apparently due to failure of recovery of FG muscle fiber area. Following reinnervation, relationships between motoneuron electrical and muscle-unit contractile properties were similar to controls. This was reflected in a degree of correspondence between motor-unit type and motoneuron type similar to normal units (84 vs. 86%, as defined by Ref. 61). There was a significantly increased proportion of type-SO muscle fibers and a decrease in the fast muscle fibers (especially type FOG) in 9 mo reinnervated MG. Together with the unchanged proportions of motor-unit types, this led to an estimate of average innervation ratios being increased in type-S motor units and decreased in type-FR units.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Properties of self-reinnervated motor units of medial gastrocnemius of cat. I. Long-term reinnervation. 371 73

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

In the intermediate layers of the rat and mouse colliculus there is a lattice-like pattern of high nicotinamide adenine dinucleotide phosphate diaphorase activity. This lattice is composed of dark bands that are 100-200 micron wide and enclose pale areas of irregular shape. A very similar lattice of high acetylcholinesterase activity is also found in the intermediate layers and this overlaps the diaphorase lattice almost completely. However, in deeper layers the enzymes have a complementary organization with high levels of one being associated with low levels of the other. It is concluded that the histochemical lattices will provide useful patterns with which to compare the terminal organization of afferent systems.
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PMID:Spatial relationship of NADPH-diaphorase and acetylcholinesterase lattices in the rat and mouse superior colliculus. 377 47

The activity of reduced nicotinamide adenine dinucleotide (NADH)-diaphorase was examined histochemically in the amygdala, cortex and sublenticular substantia innominata (nucleus basalis of Meynert) of patients with Alzheimer's disease and senile dementia of the Alzheimer type (SDAT). Senile plaques were characterized by increased enzyme levels and the presence of astrocytes highly reactive for NADH-diaphorase. In the sublenticular substantia innominata, the number of neurons positive for NADH-diaphorase was reduced in both Alzheimer's disease and SDAT, a result paralleled by a reduction of Nissl-stained cells, and this pathology was accompanied by an increase in the number of astrocytes. Intact substantia innominata somata in the former dementia, however, showed essentially normal levels of the enzyme, whereas in the SDAT patients, an abnormal distribution of NADH-diaphorase was observed frequently. It is proposed that the increased NADH-diaphorase associated with senile plaques and their accompanying astrocytes may be linked, in part, to the increased astrogliosis and decrease of neurons in the basal forebrain and that neuropathologic differences may exist between Alzheimer's disease and SDAT in terms of energy metabolism.
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PMID:Alzheimer dementia and reduced nicotinamide adenine dinucleotide (NADH)-diaphorase activity in senile plaques and the basal forebrain. 383 7

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.
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PMID:Neuropeptides and NADPH-diaphorase activity in the ascending cholinergic reticular system of the rat. 396 Mar 9

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.
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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.
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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.
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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.
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PMID:Cytochemical localization of two glycolytic dehydrogenases in white skeletal muscle. 428 29


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