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Gene Review

Gpd2  -  glycerol phosphate dehydrogenase 2,...

Mus musculus

Synonyms: AA408484, AI448216, AU021455, AW494132, GPD-M, ...
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Disease relevance of Gpd2

  • When rat hepatoma cells of clone FU5AH were exposed to 3 microM hydrocortisone (HC) for 3 days, GPDH specific activity increased greater than sixfold over control [1].

High impact information on Gpd2

  • In adipocytes, which express high levels of PPARgamma, expression of cytosolic GPDH was enhanced by PPARgamma and beta/delta agonists, while expression was decreased in PPARgamma(+/-) and PPARbeta/delta(-/-) mice [2].
  • Transactivation, gel shift, and chromatin immunoprecipitation experiments demonstrated that cytosolic GPDH is a direct PPAR target gene [2].
  • The number of GPDH-positive Bergmann glia cells associated with isolated Purkinje cells was close to that expected, based on measurements in Golgi-stained, normal cerebella of the Bergmann glia cell's domain [3].
  • The developmentally regulated enzyme sn-glycerol-3-phosphate dehydrogenase (GPDH; EC is characteristically present in relatively high levels in mature Bergmann glia of the mouse cerebellum [4].
  • This observation suggest that the loss of GPDH immunoreactivity is not a result of glial cell death [4].

Biological context of Gpd2

  • This difference in enzyme levels, which positively correlates with similar differences in the levels of hybridizable GPDH mRNA, is controlled by at least two unlinked regulatory loci and the structural gene, Gdc-1, located on chromosome 15 [5].
  • High [Ca(2+)](e) significantly inhibited differentiation marker expression including adipocyte fatty acid binding protein, and GPDH [6].
  • Then, cultures underwent a 2-fold increase in total cell number through selective multiplication of committed cells, followed by a dramatic decrease in colony-forming ability and 300- to 1000-fold raise in GPDH activity [7].
  • Rat serum induces dose-dependent rapid cell division, which coincides with accumulation of TG and increase of GPDH; for routine quantitation, TG is assayed [8].
  • To learn whether a high level of GPDH could be reinduced following down-regulation in Lc Bg, we grafted wild-type fetal Pcs into Lc cerebella [9].

Anatomical context of Gpd2

  • GPDH was also induced by glucocorticoids in cultures of hepatocytes isolated from livers of 6-day-old rats [1].
  • T3 sensitized the cells to the inhibitory action of RA; the ED50 for GPDH activity was shifted from 0.5 microM to 3 nM in cells cultured with 1.5 nM T3 [10].
  • Previous studies have shown that cytosolic glycerol-3-phosphate dehydrogenase (GPDH; EC can be induced by glucocorticoids in mammalian brain, mammary gland, and thymus, but it was thought that no induction occurred in liver [1].
  • Results here suggest that the 5' flanking region of the GPDH gene mediates the ligand-inducible regulation of GPDH, and that multiple signaling pathways converge at the 5' regulatory sequence to modulate GPDH gene expression in oligodendrocytes [11].
  • PGF(2)alpha suppressed GPDH activity and did not increase the expression of GLUT1 protein in 3T3-L1 cells treated with DEX, IBMX, and insulin [12].

Associations of Gpd2 with chemical compounds

  • Comparison of the promoter sequence for the sn-glycerol-3-phosphate dehydrogenase (GPDH, EC genes in mice and humans showed that there were three promoter domains conserved in evolution (1) [13].
  • The expression of late markers of adipocyte differentiation, such as aP2 and GPDH, was diminished and appeared to vary with the degree to which HSL was overexpressed and the cellular triglyceride content was reduced [14].
  • When BPA was absent during the first 2-day treatment period, the cultures contained 1.6 microg/microg DNA of triacylglycerol (TG), 202 mU/mg DNA of lipoprotein lipase (LPL) activity, and 462 nmol/min/mg DNA of glycerol-3-phosphate dehydrogenase (GPDH) activity [15].
  • This mutant mouse-GPDH combination was used in the present study to define the critical time period during which thyroid hormone (T4) and growth hormone (GH) are essential for maturation of Bergmann glial cells [16].
  • To determine whether glial GPDH expression requires the continued presence of Pcs in adults, we used single intracerebellar injections of kainic acid to kill Pcs in wild-type mice from 7 weeks to 11 months old [9].

Other interactions of Gpd2

  • This GPDH cDNA clone was mapped to the Gdc-1 locus by identification of a restriction enzyme polymorphism present in genomic DNA isolated from Gdc-1 congeneic lines of mice [17].

Analytical, diagnostic and therapeutic context of Gpd2

  • Immunocytochemistry showed apparently normal GPDH expression only in Bergmann glia in the immediate vicinity of surviving Purkinje cells [3].
  • GPDH expression, as determined by enzyme activity and Northern blot analysis, was reduced by about 50% in the cerebellum and brainstem of the three hypothyroid mutant mice [18].
  • Differentiation was monitored by Oil Red O staining of cytoplasmic lipid and triglyceride assay of accumulated lipid, by RT-PCR analysis of adipogenic markers, and by the activity of glycerol-3-phosphate dehydrogenase (GPDH) [6].
  • Neither mouse retinal GPDH nor brain GPDH is affected by adrenalectomy, suggesting that they are not regulated by glucocorticoids [19].


  1. Glycerol-3-phosphate dehydrogenase is induced by glucocorticoids in hepatocytes and hepatoma cells in vitro. Meyer, R.D., Preston, S.L., McMorris, F.A. J. Cell. Physiol. (1983) [Pubmed]
  2. PPARalpha governs glycerol metabolism. Patsouris, D., Mandard, S., Voshol, P.J., Escher, P., Tan, N.S., Havekes, L.M., Koenig, W., März, W., Tafuri, S., Wahli, W., Müller, M., Kersten, S. J. Clin. Invest. (2004) [Pubmed]
  3. Neuronal influence on glial enzyme expression: evidence from chimeric mouse cerebellum. Fisher, M., Mullen, R.J. Neuron (1988) [Pubmed]
  4. Neuronal influence on glial enzyme expression: evidence from mutant mouse cerebella. Fisher, M. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  5. Interacting genes control glycerol-3-phosphate dehydrogenase expression in developing cerebellum of the mouse. Kozak, L.P. Genetics (1985) [Pubmed]
  6. High extracellular calcium attenuates adipogenesis in 3T3-L1 preadipocytes. Jensen, B., Farach-Carson, M.C., Kenaley, E., Akanbi, K.A. Exp. Cell Res. (2004) [Pubmed]
  7. Commitment of 3T3-F442A cells to adipocyte differentiation takes place during the first 24-36 h after adipogenic stimulation: TNF-alpha inhibits commitment. Castro-Muñozledo, F., Beltrán-Langarica, A., Kuri-Harcuch, W. Exp. Cell Res. (2003) [Pubmed]
  8. Preadipocyte stimulating factor in rat serum: evidence for a discrete 63 kDa protein that promotes cell differentiation of rat preadipocytes in primary cultures. Li, Z.H., Lu, Z.D., Kirkland, J.L., Gregerman, R.I. J. Cell. Physiol. (1989) [Pubmed]
  9. Bergmann glia require continuous association with Purkinje cells for normal phenotype expression. Fisher, M., Trimmer, P., Ruthel, G. Glia (1993) [Pubmed]
  10. Retinoic acid decreases nuclear triiodothyronine receptor expression and impairs an early step of adipose differentiation in the thyroid hormone-sensitive mouse Ob 17 preadipocyte cell line. Teboul, M., Bismuth, J., Gharbi-Chihi, J., Vallette, A., Bonne, J., Ghiringhelli, O., Torresani, J. Endocrinology (1992) [Pubmed]
  11. Oligodendrocytes as glucocorticoids target cells: functional analysis of the glycerol phosphate dehydrogenase gene. Cheng, J.D., de Vellis, J. J. Neurosci. Res. (2000) [Pubmed]
  12. Prostaglandin F(2)alpha enhances glucose consumption through neither adipocyte differentiation nor GLUT1 expression in 3T3-L1 cells. Kamon, J., Naitoh, T., Kitahara, M., Tsuruzoe, N. Cell. Signal. (2001) [Pubmed]
  13. Tissue- and cell-specific expression of human sn-glycerol-3-phosphate dehydrogenase in transgenic mice. Birkenmeier, E.H., Hoppe, P.C., Lyford, K.A., Gwynn, B. Nucleic Acids Res. (1992) [Pubmed]
  14. Overexpression of hormone-sensitive lipase prevents triglyceride accumulation in adipocytes. Sztalryd, C., Komaromy, M.C., Kraemer, F.B. J. Clin. Invest. (1995) [Pubmed]
  15. Bisphenol A in combination with insulin can accelerate the conversion of 3T3-L1 fibroblasts to adipocytes. Masuno, H., Kidani, T., Sekiya, K., Sakayama, K., Shiosaka, T., Yamamoto, H., Honda, K. J. Lipid Res. (2002) [Pubmed]
  16. Stimulatory effects of exogenous thyroid hormone and growth hormone on sn-glycerol-3-phosphate dehydrogenase activity in the genetic-hypothyroid mutant mouse cerebellum: restricted to the second 20 days of postnatal life. Sugisaki, T., Noguchi, T. J. Neurochem. (1992) [Pubmed]
  17. Mouse sn-glycerol-3-phosphate dehydrogenase: molecular cloning and genetic mapping of a cDNA sequence. Kozak, L.P., Birkenmeier, E.H. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  18. Genetic hypothyroid mice: normal cerebellar morphology but altered glycerol-3-phosphate dehydrogenase in Bergmann glia. Sugisaki, T., Noguchi, T., Beamer, W.G., Kozak, L.P. J. Neurosci. (1991) [Pubmed]
  19. Glycerol phosphate dehydrogenase in developing retina of normal and mutant mice. McGinnis, J.F., Leveille, P.J. Curr. Eye Res. (1984) [Pubmed]
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