Disease relevance of Gpd1

• An oligodendroglial specific property, glucocorticoid regulation of glycerol-3-phosphate dehydrogenase (GPDH) levels, was inhibited in C6 rat glioma cells when 4 beta-phorbol 12-myristate 13-acetate (PMA) was added to the cultures [1].

High impact information on Gpd1

• Treatment with insulin and various concentrations of d-glucose increased mRNA levels for FAS (280%), ACC (93%), and GPDH (633%) in a dose-dependent manner (ED50 8-16 mm) [2].
• The adipose conversion was assessed by the development of lipoprotein lipase (LPL) and glycerol-3-phosphate dehydrogenase (GPDH) activities, [14C]glucose incorporation into polar and neutral lipids, triacylglycerol accumulation and lipolysis in response to isoproterenol [3].
• However, both HA and Arg exhibited significant induction on differentiation, as evidenced by increased lipoprotein lipase (LPL) and glycerol-3-phosphate dehydrogenase (GPDH) activities, as well as accelerated triacylglycerol (TG) accumulation [4].
• Surprisingly, administration of analgesic doses of morphine or the nonsteroidal antiinflammatory drugs aspirin, metamizol (dipyrone), and indomethacin also increased GPDH mRNA levels in rat spinal cord [5].
• The opioid receptor antagonist naloxone completely blocked morphine induction of GPDH but had no effect on GPDH induction by noxious heat stimulation or metamizol treatment, implicating different mechanisms of GPDH induction [5].

Biological context of Gpd1

• We demonstrate that the presence of one fa allele significantly increases lipogenesis in adipose tissue assessed by glycerol-3-phosphate dehydrogenase (GPDH) and fatty acid synthase (FAS) activities [6].
• The offspring of rats injected with metyrapone did not have raised blood pressure or GPDH activities [7].
• In contrast, carbaprostacyclin (cPGI2), a stable analogue of prostacyclin, behaves as a true adipogenic factor leading to a 4 to 5-fold increase in GPDH-specific activities with no significant effect on cell growth [8].
• The specificity of GPDH antigen-antibody reaction was determined by qualitative and quantitative immunochemical methods and by imunocytochemical controls for immunologic and methodologic sources of nonspecific reaction product [9].
• In addition, GPDH gene expression represents a glucocorticoid-dependent stress response which is rapidly increased in a dose- and stressor-dependent manner [10].

Anatomical context of Gpd1

• The activity of liver mitochondrial flavoprotein-dependent glycerol-3-phosphate dehydrogenase (GPDH) is considered a reliable marker of thyroid status in acute and short-lasting experiments [11].
• Normal optic nerve preparations possessed a high level of GPDH activity that was glucocorticoid-inducible and that increased further following axonal degeneration [12].
• Northern blot and in situ hybridization analysis confirmed the differential display results; they also showed, in a separate model of neuronal activation, that after thermal noxious stimulation of the hind-paws, a similar increase in GPDH mRNA occurs in the areas of somatotopic projection in the lumbar spinal cord [5].
• 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 [12].
• The animals that had been exposed to a maternal low-protein diet also exhibited increased glycerol-3 phosphate dehydrogenase (GPDH) activity in the hypothalamus, whereas their pyruvate kinase activity was not changed [7].

Associations of Gpd1 with chemical compounds

• We found a seven- and three-fold increase of GPDH activity in female rats after T (3) or T (4) administration, respectively, compared to euthyroid females (8.9 +/- 2.3 nmol/min/mg protein), whereas administration of methimazole reduced the enzyme activity almost to one-third of the euthyroid values [11].
• The hydrocortisone (HC) induction of glycerol phosphate dehydrogenase (GPDH; EC 1.1.1.8) in rat glial C6 cells was inhibited reversibly and in a dose-dependent manner by cytochalasin B (CB) [13].
• Replacement of corticosterone during pregnancy had no effect upon the blood pressures and GPDH activities of male offspring, but it reversed the effects of metyrapone in female offspring [7].
• Nevertheless, in all cases, induction of the GPDH gene requires adrenal steroids and new protein synthesis, as the induction was blocked in adrenalectomized rats and by cycloheximide treatment, respectively [5].
• The addition of an alternate energy source (sodium pyruvate) did not relieve the CB inhibition of GPDH induction suggesting that CB is not exerting its effect by blocking glucose utilization [13].

Analytical, diagnostic and therapeutic context of Gpd1

• Using mRNA differential display, we found that the gene for NAD(+)-dependent glycerol phosphate dehydrogenase (GPDH; EC 1.1.1.8) is induced in rat brain following seizure activity [5].
• Increases in the mRNA levels of two neuroglial markers, glutamine synthetase (EC 6.3.1.2; GS) and glycerolphosphate dehydrogenase (EC 1.1.1.8; GPDH), were observed in hydrocortisone-treated cultures of astrocytes and oligodendrocytes, respectively, and in C6 cells by Northern blot analysis and in situ hybridization [14].
• The 35,000 Da hippocampal protein co-eluted from a gel filtration column with GPDH activity [15].
• We now show by immunoprecipitation that this cytosolic protein is glycerol 3-phosphate dehydrogenase (E.C.1.1.1.8; GPDH) [16].
• However, daily administration of corticosterone to rats beginning 10 days after adrenalectomy returned hippocampal GPDH activity to normal values after 2-3 days [15].

References