Erythrocytic nicotinamide-adenine dinucleotide phosphate levels and the genetic regulation of erythrocytic glucose 6-phosphate dehydrogenase activity in the inbred mouse

1974 ◽  
Vol 11 (1) ◽  
pp. 33-40 ◽  
Author(s):  
Robert P. Erickson
Keyword(s):  
Dehydrogenase Activity ◽  
Nicotinamide Adenine Dinucleotide ◽  
Inbred Mouse ◽  
Genetic Regulation ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Glucose 6 Phosphate Dehydrogenase

scholarly journals Multiple forms with glucose 6-phosphate dehydrogenase activity in Musca domestica L. as revealed by electrophoresis on cellulose acetate gel.

1978 ◽  
Vol 26 (10) ◽  
pp. 846-854 ◽  
Author(s):  
L Cima ◽  
A Malacrida ◽  
G Gasperi ◽  
L Sacchi ◽  
A Grigolo
Keyword(s):  
Musca Domestica ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
G6pd Activity ◽  
Nicotinamide Adenine ◽  
Molecular Forms ◽  
Type I ◽  
Coenzyme Specificity ◽  
Low Sensitivity ◽  
Glucose 6 Phosphate Dehydrogenase

Single newly emerged males of Musca domestica, WHO strain, usually show five electrophoretic bands of glucose 6-phosphate dehydrogenase (G6PD) activity. Of these five molecular forms, designated with Roman numerals in order from the origin, we have considered the first three: these have been characterized with respect to their substrate and coenzyme specificity and to their sensitivity to some sulfhydryl inhibitors. The data show band III to be G6P specific, nicotinamide adenine dinucleotide phosphate dependent and to be a type I enzyme according to Kamada and Hori's classification. Bands I and II, on the other hand, show wide substrate specificity and low sensitivity to the sulfhydryl inhibitors assayed. In addition, in the absence of an exogenous substrate and in the presence of nicotinamide adenine dinucleotide as a coenzyme, fairly weak bands, which can be ascribed to the so called "nothing dehydrogenase" effect, are seen in the position I and II. Nevertheless, the data reported do not allow a clear definition of the enzymatic type corresponding to bands I and II of G6PD activity.

scholarly journals LOCALIZATION OF NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE-DEPENDENT DEHYDROGENASES IN CATECHOLAMINE-CONTAINING NEURONS OF RAT BRAIN STUDIES ON THE NUCLEUS LOCUS CERULEUS

1974 ◽  
Vol 22 (1) ◽  
pp. 20-28 ◽  
Author(s):  
F. C. KAUFFMAN ◽  
F. E. BLOOM ◽  
K. L. SIMS ◽  
V. M. PICKEL
Keyword(s):  
Brain Stem ◽  
Rat Brain ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Locus Ceruleus ◽  
Nicotinamide Adenine ◽  
High Concentration ◽  
Intense Staining ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase

Histochemical and cytochemical methods have been used to localize glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, isocitrate (nicotinamide adenine dinucleotide phosphate (NADP)) dehydrogenase and malic enzyme in the nucleus locus ceruleus and other catecholamine-containing neuronal groups of the rat brain stem. The four NADP-dependent dehydrogenases were studied by both quantitative and qualitative histochemical techniques using adjacent tissue sections. Both types of analyses were done on neuronal nuclei known to contain catecholamines in high concentration, the nucleus locus ceruleus and the superior cervical sympathetic ganglion; other known catecholamine-containing nuclei were surveyed by the cytologic technique only. There was intense staining of cell bodies and neuropil of the nucleus locus ceruleus after all four of the NADP dehydrogenase histochemical reactions. In contrast, little staining was observed in the adjacent vestibular nuclei or mesencephalic root nucleus of the trigeminal with the exception of appreciable glucose 6-phosphate dehydrogenase activity present in neuropil elements. Quantitative microchemical determinations in the nucleus locus ceruleus corroborate the histochemical results which indicated high NADP dehydrogenase activities particularly for 6-phosphogluconate dehydrogenase. This same pattern of high NADP enzyme activity as determined by combined cytochemical and quantitative chemical techniques was also observed in the superior cervical ganglion and cytochemically in other catecholamine-containing nuclei of the brain stem. Our findings suggest that a high capacity to generate or utilize nicotinamide adenine dinucleotide phosphate (reduced) may be characteristic of those neurons which either receive adrenergic terminals or synthesize catecholamines.

scholarly journals Metabolic changes in the lymphocytes during influenza

2012 ◽  
Vol 93 (4) ◽  
pp. 580-584
Author(s):  
I V Sergeeva ◽  
N I Kamzalakova ◽  
E P Tikhonova ◽  
G V Bulygin
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Tricarboxylic Acid Cycle ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Tricarboxylic Acid ◽  
Nicotinamide Adenine ◽  
Control Group ◽  
Healthy Individuals ◽  
Acid Cycle ◽  
Intracellular Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

Aim. To assess the nature and intensity of metabolic processes in lymphocytes of patients with influenza according to the activity of intracellular enzymes in comparison to the severity of the disease. Methods. Determined were the enzymatic parameters of lymphocytes of 45 patients aged 18 to 42 years with a diagnosis of «influenza». Two groups of patients were formed: with moderate (24 patients) and severe (21 patients) course of the disease. Used as controls were the values the activity of intracellular enzymes of lymphocytes of 37 practically healthy individuals of comparable age. Results. In patients with a moderately severe course of the influenza compared with the controls noted was a significant increase in activity of glucose-6-phosphate dehydrogenase (3.17±0.53 and 2.74±0.31 mkE/10 000 cells, p 0.05) and glycerol-3-phosphate dehydrogenase (57.33±±5.65 and 0.84±0.16 mkE/10 000 cells respectively, p 0.001). The activity of lactate dehydrogenase was lower in patients than in controls (0.40±0.08 and 0.84±0.08 mkE/10 000 cells respectively, p 0.001). Indicators of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate dependant isocitrate dehydrogenases in lymphocytes of patients were lower than in the controls: the first indicator in the patients was 0.17±0.02 mkE/10 000 cells, in controls - 1.95±0.25 mkE/10 000 cells (p 0.001), and for the second indicator these values were respectively 0.09±0.01 and 31.02±±2.20 mkE/10 000 cells (p 0.001). In patients with a moderately severe course of influenza the activity of nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate dependant glutamate dehydrogenases was significantly higher compared with healthy individuals: 63.67±5.32 and 0.34±0.06 mkE/10 000 cells, 1.45±0.18 and 0.11±0.02 mkE/10 000 cells respectively (p 0.001). The activity of nicotinamide adenine dinucleotide dependant malate dehydrogenase in patients was equal to 86.46±12.30 mkE/10 000 cells (in the control group 84.16±13.70 mkE/10 000 cells), and the activity of nicotinamide adenine dinucleotide phosphate dependant malate dehydrogenase was equal to 1.34±±0.25 mkE/10 000 cells (in the control group 0.33±0.07 mkE/10 000 cells, p 0.001). The activity of glutathione reductase was also higher in patients with the moderately severe course of the influenza: 5.86±0.25 mkE/10 000 cells, while the value in healthy individuals was 1.28±0.30 mkE/10 000 cells (p 0.001). In the group of patients with a severe course of influenza the activity of almost all (except for glucose-6-phosphate dehydrogenase) enzymes was higher than during the moderately severe course of disease. Conclusion. At the peak of the diseases noted were opposite changes in the activity of reactions of the pentose phosphate cycle and glycolysis. With a high functional load on the cells there is a significant reduction in the intensity of the reactions of the initial phase of the tricarboxylic acid cycle, which reduces the energy efficiency of the cycle, while the intense influx of metabolites to supply the tricarboxylic acid cycle with substrates of the amino acid metabolism provides enhanced transport of amino acids into the lymphocytes.

THE EFFECT OF PROGESTERONE, GLUCOSE-6-PHOSPHATE DEHYDROGENASE, ADRENOCORTICOTROPHIC HORMONE AND METYRAPONE ON ADRENOCORTICAL SECRETION OF RAT ADRENAL GLANDS CULTURED UNDER HYPERBARIC OXYGEN

1969 ◽  
Vol 43 (2) ◽  
pp. 265-270 ◽  
Author(s):  
R. E. COUPLAND ◽  
S. BISWAS ◽  
J. D. B. MacDOUGALL
Keyword(s):  
Hyperbaric Oxygen ◽  
Nicotinamide Adenine Dinucleotide ◽  
Adrenal Glands ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Secretion Rate ◽  
Nicotinamide Adenine ◽  
Adrenocorticotrophic Hormone ◽  
Organ Cultures ◽  
Steroid Secretion ◽  
Glucose 6 Phosphate Dehydrogenase

SUMMARY Exposure of organ cultures of rat adrenal glands to hyperbaric oxygen at 2 atm. increases steroid output during the first 24 hr. but the secretion rate falls after that time. This reduction is partially prevented by the addition of progesterone and during the period 24–48 hr. completely prevented by the addition of progesterone together with glucose-6-phosphate, glucose-6-phosphate dehydrogenase and nicotinamide adenine dinucleotide phosphate. Addition of bovine and synthetic adrenocorticotrophin to cultures maintained in hyperbaric oxygen results in a further increase in steroid secretion during the period 0–6 hr. Addition of metyrapone results in a reduction in the output of corticosterone, 18-hydroxycorticosterone and aldosterone.

scholarly journals The role of nicotinamide–adenine dinucleotide phosphate-dependent malate dehydrogenase and isocitrate dehydrogenase in the supply of reduced nicotinamide–adenine dinucleotide phosphate for steroidogenesis in the superovulated rat ovary

1970 ◽  
Vol 117 (1) ◽  
pp. 73-83 ◽  
Author(s):  
A. P. F. Flint ◽  
R. M. Denton
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Tissue Homogenate ◽  
Kinetic Properties ◽  
Rat Ovary ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Effect Of Glucose

1. Superovulated rat ovary was found to contain high activities of NADP–malate dehydrogenase and NADP–isocitrate dehydrogenase. The activity of each enzyme was approximately four times that of glucose 6-phosphate dehydrogenase and equalled or exceeded the activities reported to be present in other mammalian tissues. Fractionation of a whole tissue homogenate of superovulated rat ovary indicated that both enzymes were exclusively cytoplasmic. The tissue was also found to contain pyruvate carboxylase (exclusively mitochondrial), NAD–malate dehydrogenase and aspartate aminotransferase (both mitochondrial and cytoplasmic) and ATP–citrate lyase (exclusively cytoplasmic). 2. The kinetic properties of glucose 6-phosphate dehydrogenase, NADP–malate dehydrogenase and NADP–isocitrate dehydrogenase were determined and compared with the whole-tissue concentrations of their substrates and NADPH; NADPH is a competitive inhibitor of all three enzymes. The concentrations of glucose 6-phosphate, malate and isocitrate in incubated tissue slices were raised at least tenfold by the addition of glucose to the incubation medium, from the values below to values above the respective Km values of the dehydrogenases. Glucose doubled the tissue concentration of NADPH. 3. Steroidogenesis from acetate is stimulated by glucose in slices of superovulated rat ovary incubated in vitro. It was found that this stimulatory effect of glucose can be mimicked by malate, isocitrate, lactate and pyruvate. 4. It is concluded that NADP–malate dehydrogenase or NADP–isocitrate dehydrogenase or both may play an important role in the formation of NADPH in the superovulated rat ovary. It is suggested that the stimulatory effect of glucose on steroidogenesis from acetate results from an increased rate of NADPH formation through one or both dehydrogenases, brought about by the increases in the concentrations of malate, isocitrate or both. Possible pathways involving the two enzymes are discussed.

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