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Results for “GLYCEROLPHOSPHATE DEHYDROGENASE”

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At least 37 records · Page 2Linked to original sources
PubMed1979

[Nonspecific esterase and alpha-glycerolphosphate dehydrogenase activity and the fat content in the regenerating chicken liver].

The data on histochemical study of changes in the activity of esterases, alpha-glycerophosphate dehydrogenase and the fat content in the chick regenerating liver are presented. The accumulation of the fat in hepatocytes during the early periods of regeneration (1--5th day of the experiment) is partially conditioned by the reduction of the activity of nonspecific esterases. The maximal liver steatosis is accompanied also by an increase in the activity of alpha-glycerophosphate dehydrogenase which indicates intensification of glycolysis and synthesis of triacylglycerines (liver spare lipids) during regeneration.

Animals↗
PubMed2002

Expression of glucose transporter-2, glucokinase and mitochondrial glycerolphosphate dehydrogenase in pancreatic islets during rat ontogenesis.

To gain better insight into the insulin secretory activity of fetal beta cells in response to glucose, the expression of glucose transporter 2 (GLUT-2), glucokinase and mitochondrial glycerol phosphate dehydrogenase (mGDH) were studied. Expression of GLUT-2 mRNA and protein in pancreatic islets and liver was significantly lower in fetal and suckling rats than in adult rats. The glucokinase content of fetal islets was significantly higher than of suckling and adult rats, and in liver the enzyme appeared for the first time on about day 20 of extrauterine life. The highest content of hexokinase I was found in fetal islets, after which it decreased progressively to the adult values. Glucokinase mRNA was abundantly expressed in the islets of all the experimental groups, whereas in liver it was only present in adults and 20-day-old suckling rats. In fetal islets, GLUT-2 and glucokinase protein and their mRNA increased as a function of increasing glucose concentration, whereas reduced mitochondrial citrate synthase, succinate dehydrogenase and cytochrome c oxidase activities and mGDH expression were observed. These findings, together with those reported by others, may help to explain the decreased insulin secretory activity of fetal beta cells in response to glucose.

Animals↗
PubMed1994

[The alpha-glycerolphosphate dehydrogenase and adenosinetriphosphatase activity of the peripheral blood lymphocytes in diabetics (a cytochemical determination)].

Decrease in activity of alpha-GPDG and ATP-ase observed in peripheral lymphocytes of patients with diabetes mellitus correlated well severity of the disease. The lowest indices of enzymatic activity were registered in patients with grave diabetes complicated by angiopathies, foot gangrene, and purulent inflammatory processes. Compensation of carbohydrates metabolism and improvement of clinical picture were accompanied by the trend to normalization of enzymes' activity. Dynamic study of alpha-GPDG and ATP-ase in patients with diabetes mellitus allows to evaluate degree of hypoxia, comprehend the nature of compensation mechanisms and assess effectiveness of the treatment.

Adenosine Triphosphatases↗
PubMedDate not supplied

[alpha-glycerolphosphate dehydrogenase activity in rabbit organs and tissues in various endocrine disorders].

Activity of alpha-glycerophosphate dehydrogenase (GPDG) from rabbit tissues was distinctly decreased in hypothyroidism and increased in hyperthyroidism. In alloxane diabetes and after administration of high doses of insulin the GPDG activity, and especially the activity of its mitochondrial form, was markedly decreased in kidney and heart tissues; it was unaltered or slightly increased in liver tissue and sceletal muscles, as compared with control. The hormonal regulation of the GPDG activity is a complicated process, in which are involved not only the hormones of thyroid gland but also hormones of other endocrine glands.

11-Hydroxycorticosteroids↗
PubMed1980

[Characteristics of the NAD-dependent alpha-glycerolphosphate dehydrogenase isoenzymes from vertebrate and human muscles according to polyacrylamide gel electrophoretic and isoelectric focusing data].

Electrophoresis and isoelectric focusing in polyacrylamide gel were used to demonstrate the presence of 5 molecular forms of alpha-glycerophosphate dehydrogenase (E. C. I. I. I. 8, alpha-GDH) in the cytoplasm of some vertebrata skeletal muscles. Assay of alpha-GDH isozyme distribution in the muscles marked by the prevalent type of oxidation disclosed the higher activity of the cathodic forms--alpha-GDH4 and alpha-GDH5--in the white muscle (m. quadratus lumborum) as compared with the red one (m. soleus). It is suggested that the study of alpha-GDH molecular form distribution may serve as an objective criterion for changes in the ratio of the aerobic and anaerobic processes in animal tissues under different states of animal body.

Adult↗
PubMed1982

Effect of procarbazine treatment of mice on alpha-glycerolphosphate dehydrogenase activity and frequency of selected abnormalities in sperm.

The in situ activity of mitochondrial alpha-glycerol phosphate dehydrogenase (alpha-GPD) as well as 2 specific sperm abnormalities [headless and disorganization of the mitochondria assembly (PL-type)] have been studied in sperm from mice treated with single doses of procarbazine (100, 200, 400, 600 and 800 mg/kg) at intervals up to 55 days after treatment. The frequency of sperm without active alpha-GPD and the frequency of the morphology variants increased with increasing dose of procarbazine. The variance in the level of alpha-GPD among sperm with active enzyme and the variance between animals also increased with increasing dose. The lowest effective dose was 200 mg/kg and there were no observable effects 85 days after treatment.

Animals↗
PubMed1982

Evidence for glucocorticoid target cells in the rat optic nerve. Hormone binding and glycerolphosphate dehydrogenase induction.

Biochemical evidence suggests that neuroglia are responsive to glucocorticoids, yet previous studies of glucocorticoid localization have typically failed to demonstrate significant uptake by neuroglial cells. To further investigate this problem, we measured glycerol-3-phosphate dehydrogenase (GPDH) activity and glucocorticoid receptor binding capacity in normal rat optic nerves and in those undergoing Wallerian (axonal) degeneration. Binding studies were also performed on hippocampus and anterior pituitary for comparison purposes. Normal optic nerve preparations possessed a high level of GPDH activity that was glucocorticoid-inducible and that increased further following axonal degeneration. Antibody inactivation experiments demonstrated the presence of more enzyme molecules in the degenerating nerve preparations. correlative immunocytochemical studies found GPDH-positive reaction product only in morphologically identified oligodendrocytes, a result that is consistent with the previously reported localization of this enzyme in rat brain. Optic nerve cytosol fractions displayed substantial high-affinity binding of both dexamethasone (DEX) and corticosterone (CORT) that, like GPDH, was elevated approximately two fold in degenerating nerves. Finally, in vivo accumulation of [3H]DEX and [3H]CORT by optic nerve and other myelinated tracts was examined using nuclear isolation and autoradiographic methods. Although neither steroid was found to be heavily concentrated by these tissues in vivo, a small preference for DEX was observed in the nuclear uptake experiments. These results are discussed in terms of the hypothesis that glial cells are targets for glucocorticoid hormones.

Adrenalectomy↗