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Results for “GLYCEROLPHOSPHATE DEHYDROGENASE”

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At least 19 recordsLinked to original sources
PubMed1972

Genetic control of -glycerolphosphate dehydrogenase in mouse brain.

Activity of alpha-glycerolphosphate dehydrogenase (EC 1.1.1.8), linked to cytoplasmic nicotinamide adenine dinucleotide, is higher in brains of BALB/cJ mice than in brains of C57BL/6J mice. The magnitude of the difference is dependent on both the age and brain region of the mice. Maximal differences are observed at 20 days of age and are detected in the cerebellum, with only marginal differences occurring in other brain regions. Kidney and liver of BALB/cJ mice have higher enzyme activity than those of C57BL/6J mice, whereas muscle-enzyme activity is lower in BALB/cJ mice than in C57BL/6J mice. In addition to differences in activity, alpha-glycerolphosphate dehydrogenase in BALB/cJ mice is more sensitive to heat denaturation. The half-life for the enzyme at 50 degrees in BALB/cJ, (BALB/cJ x C57BL/6J)F(1) hybrid, and C57BL/6J mice is 1, 1.7, and 3 min, respectively. Genetic analysis of the mode of inheritance of the heat-sensitive enzyme reveals that the trait is determined by a single autosomal gene. Genetic analysis of the activity of alpha-glycerolphosphate dehydrogenase in the cerebellum indicates that the mechanism of inheritance for this trait involves two or more genes and that one of these genes also confers heat sensitivity on the enzyme. The affect of these genes on enzyme activity is codominant and additive.

Animals↗
PubMed1980

Immunological and biochemical analysis of a null mutant of alpha-glycerolphosphate dehydrogenase from Drosophila melanogaster.

A Drosophila null mutant(BO-1-4) of alpha-glycerolphosphate dehydrogenase induced by ethylmethane sulfonate(EMS) was analyzed by double immunodiffusion, enzyme immunoinactivation, immunoelectrophoresis and two-dimensional electrophoresis. Based on all the immunological evidence, this mutant appears to express no protein that can cross-react with the antiserum specific to alpha-glycerolphosphate dehydrogenase. A protein spot corresponding to alpha-glycerolphosphate dehydrogenase was identified on two-dimensional gels of the soluble fly homogenates. The absence of this protein spor on two-dimensional gels of this null mutant further supported the immunological data. The activities of seven other enzymes in the related metabolic pathways were determined for the mutant and the control Drosophila. The null mutant does not show significant alterations in activities of these enzymes. The relationship between the deficiency of this enzyme and the inability for the sustained flight of the null mutant was discussed in terms of cellular metabolic regulations.

Alcohol Oxidoreductases↗
PubMed1979

Partial purification, substrate specificity and regulation of alpha-L-glycerolphosphate dehydrogenase from Saccharomyces carlsbergensis.

alpha-L-Glycerolphosphate dehydrogenase (sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase, EC 1.1.1.8) from Saccharomyces carlsbergensis was purified 400-fold. The enzyme preparation is free of interfering activities, such as glyceraldehyde phosphate dehydrogenase, alcohol dehydrogenase, triose phosphate isomerase and glycerolphosphatase. At pH 7.0 it is specific for NADH (Km = 0.027 mM with 0.8 mM dihydroxyacetone phosphate) and dihydroxyacetone phosphate (Km = 0.2 mM with 0.2 mM NADH). Between pH 5.0 and 6.0 the enzyme functions with NADPH, but only at 7% of the rate with NADH. Various anions (I- greater than SO42- greater than Br- greater than Cl-) act as inhibitors competing with the substrate dihydroxyacetone phosphate. Inorganic phosphate (Ki = 0.1 mM), pyrophosphate and arsenate are strong inhibitors. The nucleotides ATP and ADP are also inhibitory, but their action seems to be of the same type as the general anion competition (Ki = 0.73 mM for ATP). The results are consistent with the notion that the enzyme may regulate the redox potential of the NAD+/NADH couple during fermentation.

Adenine Nucleotides↗
PubMed1982

Glycerolphosphate dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase and carbonic anhydrase activities in oligodendrocytes and myelin: comparisons between species and CNS regions.

Oligodendrocytes isolated from bovine white matter had higher specific activities of glycerolphosphate dehydrogenase (GPDH) and glucose-6-phosphate dehydrogenase (G6PDH) than were observed in homogenates of white matter or gray matter from bovine brains, whereas the activity of lactate dehydrogenase (LDH) was lower in the cells than in the homogenates. These observations suggest that G6PDH, as well as GPDH, is an oligodendrocyte-enriched enzyme. The 3 enzymes were also measured in myelin from bovine brains, rat spinal cords, and mouse brains, and, for each enzyme, the relative specific activity (RSA) in myelin was calculated by dividing the specific activity in myelin by the specific activity in the respective starting homogenate. Of the 3 enzymes, GPDH, G6PDH and LDH, the RSA of G6PDH was highest, at 0.26, in the bovine myelin, whereas the RSAs of GPDH were highest, at approximately 0.20, in the myelin from rat spinal cords and mouse brains. Carbonic anhydrase was also measured in the myelin from the rodent tissues, and significantly higher RSAs, at 0.43-1.06, were obtained. The finding that carbonic anhydrase consistently has higher concentrations than either G6PDH or GPDH in myelin suggests that the latter are restricted, in the myelin sheath, to regions in which oligodendroglial cytoplasm is enclosed, whereas carbonic anhydrase is distributed more broadly in the myelin membranes. A developmental increase in GPDH in the rat spinal cord is also reported.

Aging↗
PubMed1995

Glucocorticoid regulation of glycerolphosphate dehydrogenase expression in the developing rat brain.

Glucocorticoid regulation of glycerolphosphate dehydrogenase (GPDH) activity and gene expression in the developing rat brain appears complex throughout the postnatal developmental period and attains the adult pattern after the first month of life. GPDH enzyme activity is higher in the limbic system than in the cerebral cortex of intact young animals. Adrenalectomy of young rats, before the first month of life, does not affect GPDH enzyme activity in the brain areas mentioned above, while in the adult animals it results in a statistically significant decrease in activity. Furthermore, "adult type" glucocorticoid responsivity of GPDH enzyme activity is attained in the developing limbic system earlier--by day 40 of life--than in the cerebral cortex. During the first month of life, GPDH basal mRNA levels are increased in the absence of glucocorticoids, in both the limbic system and the cortex, in contrast to the effect of adrenalectomy in the adults, where GPDH mRNA levels are decreased in the absence of the adrenals. The observed pattern of glucocorticoid regulation of GPDH during development in the rat is discussed in relation to the possible existence of various levels of regulation of GPDH gene and enzyme activity.

Animals↗
PubMed1991

Depletion of glutathione interferes with induction of glycerolphosphate dehydrogenase in the brains of young rats.

In the rat brain hydrocortisone induces the enzyme, glycerolphosphate dehydrogenase (GPDH), during the first postnatal week. The present studies focused on a hypothetical role for glutathione-S-transferase (GST) in that phenomenon. Two forms of GST, Yb and Yp, had been detected in glial cells in mature rat brains, and it was suggested that they might function in hormone transport. Now GSTs have also been observed in the brains of 1-day-old rats. Two glutathione-depleting agents, buthionine sulfoximine and cyclohexene-1-one, were administered to rats, along with hydrocortisone, during the first postnatal week. Hydrocortisone or a depleting agent alone was administered to control animals. During the early days of the experiment there were lower GPDH specific activities in brains from the animals given hydrocortisone plus a depleting agent than in those from animals given hydrocortisone alone. Depleting agents alone did not affect the specific activities of GPDH. It is suggested that one function of the GST in rat brain is transport of hydrocortisone between or within glial cells.

Aging↗
PubMed1975

Unusual increase in mitochondrial glycerolphosphate dehydrogenase activity in primary cultures of rat liver cells.

Primary cultures of neonatal rat liver cells show an increase in the activity of mitochondrial glycerolphosphate dehydrogenase between the second and tenth day of cultivation. At the end of cultivation the activity level exceeded that of liver tissue in vivo. Replacement of normal serum by hypothyroid serum or addition of triiodothyronine to the medium did not influence significantly the enzyme activity in vitro, in contrast to the very marked effects of thyroid hormones observed in vivo.

Animals↗
PubMed1981

Further observations on the hormonal regulation of alpha-glycerolphosphate dehydrogenase in rat mammary gland: a possible role for prolactin and thyrotropin.

The roles of prolactin and thyrotropin (TSH) in the regulation of alpha-glycerolphosphate dehydrogenase (alpha-GPDH) activity in rat mammary gland were investigated by the administration of thyroid releasing hormone, bromocriptine, prolactin, TSH and triiodothyronine (T3). TRH administration failed to induce alterations in the glands from intact animals but stimulated the activity in castrated and adrenalectomized animals. Bromocriptine administration was without any effect in either group of animals. Administration of ovine prolactin to hypophysectomized rats did not affect the activity, on the other hand, treatment with either TSH or T3 resulted in a highly significant increase in the activity. Combined administration of prolactin and TSH to hypophysectomized animals showed that prolactin is capable of partially inhibiting the TSH-induced increase. It is suggested that glucocorticoids exert primary control over the enzyme's activity with the pituitary hormones only playing a permissive role in its regulation.

Adrenalectomy↗
PubMed1987

The effects of interferons on the activity of alpha-glycerolphosphate dehydrogenase in benign prostatic hyperplasia cells in primary culture.

Human benign prostatic hyperplasia (BPH) tissues were obtained from patients undergoing transurethral resection of the prostate and viable cells from these were successfully maintained in primary cultures grown on collagen gel. The prostatic origin of the cells was confirmed by the measurement of prostate specific acid phosphatase and by scanning and transmission electron microscopy before and after immunostaining with human prostate specific antigen-antibody. The cell cultures were treated with various interferons (IFNs), both in the presence and absence of testosterone propionate (TP), for 72 hours and the activities of seven enzymes of carbohydrate metabolism were estimated in the cytosolic fraction of the cells. Treatment with TP induced a significant decrease in the activity of alpha-glycerolphosphate dehydrogenase (alpha-GPDH). Using this enzyme activity as a marker, the effects of various types of IFNs were investigated. IFN-alpha (wellferon) increased the activity of the enzyme both in the presence of one microgram./ml. of TP and in its absence whereas IFN-gamma inhibited the activity under similar conditions. The effect of treatment with IFN-beta in the presence of TP was biphasic in that there was an increase in the activity of the enzyme at the lowest concentration while at higher concentrations an inhibition of enzymic activity was observed. In the absence of TP IFN-beta inhibited the activity. The significance of these findings in terms of the clinical usefulness of IFNs is discussed and it is postulated that IFN-alpha (wellferon) might be effective in the treatment of metastatic carcinoma of the prostate in selected patients.

Cells, Cultured↗