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Gene Review

GPD1  -  glycerol-3-phosphate dehydrogenase 1...

Homo sapiens

Synonyms: GPD-C, GPDH-C, HTGTI
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Disease relevance of GPD1

  • These results suggest that GRB14, GPD1, and GDF8 are weight loss-responsive genes in skeletal muscle and that the observed transcriptional modulation of these would be expected to improve insulin signaling, decrease triglyceride synthesis, and increase muscle mass, respectively, with weight loss [1].

High impact information on GPD1

  • Surprisingly, deletion of the evolutionarily conserved fat-specific elements (FSE) in the proximal promoter region failed to reveal any alterations in GPD1 expression that were specific for either white or brown adipose tissue [2].
  • Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes the reversible biological conversion of dihydroxyacetone (DHAP) to glycerol-3-phosphate [3].
  • Expression of the GPD1 and GPP2 orthologues and glycerol retention during growth of Debaryomyces hansenii at high NaCl concentrations [4].
  • Transcription of gpd1 could be detected during vegetative growth under both aerobic and anaerobic conditions, whereas neither gpd2 nor gpd3 transcription was detected, indicating that gpd1 is the major transcribed gpd gene [5].
  • Cloning of glyceraldehyde-3-phosphate dehydrogenase-encoding genes in Mucor circinelloides (Syn. racemosus) and use of the gpd1 promoter for recombinant protein production [5].

Biological context of GPD1

  • 3. Analysis of the segregation of the human liver-specific enzymes in these hybrids led to the assignment of human GPT to chromosome 8 (previously reported, Kielty, Povey & Hopkinson, 1982) and suggests the assignment of human GPD1 to chromosome 12 [6].
  • Conserved regulatory sequences were found in both the 5' and 3' flanking regions of GPD1 [7].
  • The size (approximately 1300 nucleotides) of the single GPD1 transcript was consistent with the length (1011 bp) of the open reading frame [7].
  • Positions of four introns found in GPD1 were conserved in the corresponding Aspergillus nidulans gpdA gene (which is known to have three additional introns absent in GPD1) [7].

Anatomical context of GPD1


Associations of GPD1 with chemical compounds

  • The steady state level of GPD1 mRNA is 14-fold greater than that of the constitutively-expressed TRP1 gene (encoding a tryptophan biosynthesis enzyme) indicating that GPD1 has a stronger promoter and/or a more stable mRNA [8].
  • The gpd1 promoter was successfully used for recombinant expression of genes of both homologous (crgA encoding a regulator of carotene biosynthesis) and heterologous (gox1 from Aspergillus niger encoding glucose oxidase; GOX) nature [5].
  • The functionality and regulatory properties of the promoter of the M. circinelloides gpd1 gene (which codes for glyceraldehyde-3P-dehydrogenase) were demonstrated in R. pusillus using geneticin selection [9].
  • Monascus purpureus was transformed into hygromycin B resistance with hygromycin B phosphotransferase (hph) fused to Aspergillus nidulans trpC or a putative Monascus purpureus gpd1 promoter by electroporation [10].

Other interactions of GPD1

  • Under conditions that repressed endogenous beta-galactosidase expression, beta-galactosidase activity in transformants was constitutive and required the GPD1, TRP1 or PRO1 expression signals [8].
  • GPD1 (encoding glyceraldehyde-3-phosphate dehydrogenase) is a constitutively expressed gene in Cochliobolus heterostrophus that produces a single transcript [8].

Analytical, diagnostic and therapeutic context of GPD1


  1. GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle. Park, J.J., Berggren, J.R., Hulver, M.W., Houmard, J.A., Hoffman, E.P. Physiol. Genomics (2006) [Pubmed]
  2. 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]
  3. Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1). Ou, X., Ji, C., Han, X., Zhao, X., Li, X., Mao, Y., Wong, L.L., Bartlam, M., Rao, Z. J. Mol. Biol. (2006) [Pubmed]
  4. Expression of the GPD1 and GPP2 orthologues and glycerol retention during growth of Debaryomyces hansenii at high NaCl concentrations. Gori, K., Mortensen, H.D., Arneborg, N., Jespersen, L. Yeast (2005) [Pubmed]
  5. Cloning of glyceraldehyde-3-phosphate dehydrogenase-encoding genes in Mucor circinelloides (Syn. racemosus) and use of the gpd1 promoter for recombinant protein production. Wolff, A.M., Arnau, J. Fungal Genet. Biol. (2002) [Pubmed]
  6. Regulation of expression of liver-specific enzymes. III. Further analysis of a series of rat hepatoma X human somatic cell hybrids. Kielty, C.M., Povey, S., Hopkinson, D.A. Ann. Hum. Genet. (1982) [Pubmed]
  7. Structure of the Cochliobolus heterostrophus glyceraldehyde-3-phosphate dehydrogenase gene. Van Wert, S.L., Yoder, O.C. Curr. Genet. (1992) [Pubmed]
  8. Relative strengths of promoters from Cochliobolus heterostrophus. Van Wert, S.L., Yoder, O.C. Curr. Genet. (1994) [Pubmed]
  9. A multicopy vector system for genetic studies in Mucor circinelloides and other zygomycetes. Appel, K.F., Wolff, A.M., Arnau, J. Mol. Genet. Genomics (2004) [Pubmed]
  10. Genetic transformation of Monascus purpureus DSM1379. Kim, J.G., Choi, Y.D., Chang, Y.J., Kim, S.U. Biotechnol. Lett. (2003) [Pubmed]
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