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Gene Review

GAPDH  -  glyceraldehyde-3-phosphate dehydrogenase

Sus scrofa

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Disease relevance of GAPDH


High impact information on GAPDH

  • The effect of glucose on sarcolemmal K(ATP) channels was mediated by the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase and consequent generation of 1,3-bisphosphoglycerate [5].
  • These systems are analogous to, but more complex than, those in glyceraldehyde-3-phosphate dehydrogenase and papain where a single thiol and a histidine residue in a relatively apolar milieu form a thiolate-imidazolium ion pair which is favored over the thiol-imidazole prototropic tautomer [6].
  • Strong transcriptional activity was found for the ubiquitin and heat shock protein (hsp27, hsp70) genes, and for PAI-1 and GAPDH [7].
  • Amino acid sequence analysis of the radioactive peptide gave Ile-Val-Ser-Asn-Ala-Ser-X-Thr-Thr-Asn-(...). This sequence is identical to the highly conserved region from Ile-143 to Asn-152 in pig muscle GAPDH, except for the active site Cys-149 to which the tetrahydropentalenolactone was covalently bound [8].
  • Molecular modeling was used to compare both pentalenolactone (3) and heptelidic acid (4), a mechanistically related inactivator of GAPDH, with the normal substrate, glyceraldehyde 3-phosphate (1) [8].

Chemical compound and disease context of GAPDH


Biological context of GAPDH

  • Regardless of the transformation or editing procedures for outliers applied, there was negligible genetic variation for the expression of target genes relative to GAPDH [11].
  • The GAPDH protein of S. suis seems to be involved in the first steps of the bacterial adhesion to host cells [1].
  • Because adhesion to host cells may be important in the carrier state, this study was undertaken to characterize a 39 kDa surface protein identified as a glyceraldehyde-3-phosphate dehydrogenase (GAPDH), possibly implicated in the adhesion of the bacteria [1].
  • One of the B. stearothermophilus ACE inhibitors BG-1, was the GAPDH peptide 68-77 (Gly-Lys-Glu-Ile-Ile-Val-Lys-Ala-Glu-Arg, IC50: 32 microM) [2].
  • In comparison to the amino acid sequence of glyceraldehyde-3-phosphate dehydrogenase from other species, this peptide is in a highly conserved region and is part of the active site of the enzyme [12].

Anatomical context of GAPDH


Associations of GAPDH with chemical compounds


Other interactions of GAPDH

  • Notably, PBMC derived from immune and naive pigs constitutively produced relatively high amounts of IL-10-specific mRNA, exceeding that of GAPDH mRNA, independently of the addition of viral antigen or the mitogen concanavalin A (Con A) [20].
  • In contrast, mRNA levels coding for type I collagen, fibronectin and GAPDH (used as control of cellular activity) were not modified [21].
  • This is a simple method that allows reliable determination of the differing regulation of cytokine mRNAs specific for porcine interleukin (IL)-2, -4 and -10, interferon gamma (IFN-gamma) and the housekeeping gene, GAPDH, as an endogenous control [20].
  • To determine if suppression was at the level of IFN-alpha transcription, quantitative RT-PCR was performed for IFN-alpha mRNA and compared to GAPDH and cyclophilin mRNA quantification [22].
  • The effect of MCWE on alveolar macrophage tumor necrosis factor alpha (TNF-alpha) and interleukin-1beta (IL-1beta) gene transcription, as determined by a reverse transcription-PCR assay standardized with the endogenous glyceraldehyde-3-phosphate dehydrogenase gene, was also investigated [23].

Analytical, diagnostic and therapeutic context of GAPDH


  1. Cloning and purification of the Streptococcus suis serotype 2 glyceraldehyde-3-phosphate dehydrogenase and its involvement as an adhesin. Brassard, J., Gottschalk, M., Quessy, S. Vet. Microbiol. (2004) [Pubmed]
  2. Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase as a source of angiotensin-converting enzyme inhibitors. Kohama, Y., Nakagawa, T., Oka, H., Okuno, Y., Mimura, T., Tsujibo, H., Inamori, Y., Tsurutani, R., Nagata, K., Tomita, K. Agric. Biol. Chem. (1990) [Pubmed]
  3. Effects of treatment with pyruvate and tromethamine in experimental myocardial ischemia. Liedtke, A.J., Nellis, S.H., Neely, J.R., Hughes, H.C. Circ. Res. (1976) [Pubmed]
  4. mRNA expression of glycolytic enzymes and glucose transporter proteins in ischemic myocardium with and without reperfusion. Feldhaus, L.M., Liedtke, A.J. J. Mol. Cell. Cardiol. (1998) [Pubmed]
  5. High glucose regulates the activity of cardiac sarcolemmal ATP-sensitive K+ channels via 1,3-bisphosphoglycerate: a novel link between cardiac membrane excitability and glucose metabolism. Jovanović, S., Jovanović, A. Diabetes (2005) [Pubmed]
  6. Titration studies on the active sites of pig heart lipoamide dehydrogenase and yeast glutathione reductase as monitored by the charge transfer absorbance. Sahlman, L., Williams, C.H. J. Biol. Chem. (1989) [Pubmed]
  7. Changes in gene expression following short coronary occlusions studied in porcine hearts with run-on assays. Knöll, R., Arras, M., Zimmermann, R., Schaper, J., Schaper, W. Cardiovasc. Res. (1994) [Pubmed]
  8. Inhibition of glyceraldehyde-3-phosphate dehydrogenase by pentalenolactone. 2. Identification of the site of alkylation by tetrahydropentalenolactone. Cane, D.E., Sohng, J.K. Biochemistry (1994) [Pubmed]
  9. Effects of excess glucose and insulin on glycolytic metabolism during experimental myocardial ischemia. Liedtke, A.J., Hughes, H.C., Neely, J.R. Am. J. Cardiol. (1976) [Pubmed]
  10. Succinylation of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. A reactive threonine residue in the apoenzyme. Allen, G., Harris, J.I. Eur. J. Biochem. (1976) [Pubmed]
  11. The heritability of the expression of two stress-regulated gene fragments in pigs. Kerr, C.A., Bunter, K.L., Seymour, R., Shen, B., Reverter, A. J. Anim. Sci. (2005) [Pubmed]
  12. Identification of the arylazido-beta-alanyl-NAD+-modified site in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase by microsequencing and fast atom bombardment mass spectrometry. Chen, S., Lee, T.D., Legesse, K., Shively, J.E. Biochemistry (1986) [Pubmed]
  13. Analysis of the binding of glyceraldehyde-3-phosphate dehydrogenase to microtubules, the mechanism of bundle formation and the linkage effect. Somers, M., Engelborghs, Y., Baert, J. Eur. J. Biochem. (1990) [Pubmed]
  14. Alteration of gene expression for glycolytic enzymes in aerobic and ischemic myocardium. Liedtke, A.J., Lynch, M.L. Am. J. Physiol. (1999) [Pubmed]
  15. Follicle-stimulating hormone increases concentrations of messenger ribonucleic acid encoding cytochrome P450 cholesterol side-chain cleavage enzyme in primary cultures of porcine granulosa cells. Urban, R.J., Garmey, J.C., Shupnik, M.A., Veldhuis, J.D. Endocrinology (1991) [Pubmed]
  16. Production of (S)-3-chlorolactaldehyde from (S)-alpha-chlorohydrin by boar spermatozoa and the inhibition of glyceraldehyde 3-phosphate dehydrogenase in vitro. Stevenson, D., Jones, A.R. J. Reprod. Fertil. (1985) [Pubmed]
  17. Role of lysine residues in the binding of glyceraldehyde-3-phosphate dehydrogenase to human erythrocyte membranes. Eby, D., Kirtley, M.E. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
  18. Inactivation of glyceraldehyde-3-phosphate dehydrogenase by a reactive metabolite of acetaminophen and mass spectral characterization of an arylated active site peptide. Dietze, E.C., Schäfer, A., Omichinski, J.G., Nelson, S.D. Chem. Res. Toxicol. (1997) [Pubmed]
  19. Effects of thermal denaturation on protein glycation. Seidler, N.W., Yeargans, G.S. Life Sci. (2002) [Pubmed]
  20. T helper 1-type cytokine transcription in peripheral blood mononuclear cells of pseudorabies virus (Suid herpesvirus 1)-primed swine indicates efficient immunization. Fischer, T., Büttner, M., Rziha, H.J. Immunology (2000) [Pubmed]
  21. Expression of fibronectin and interstitial collagen genes in smooth muscle cells: modulation by low molecular weight heparin fragments and serum. Asselot-Chapel, C., Combacau, L., Labat-Robert, J., Kern, P. Biochem. Pharmacol. (1995) [Pubmed]
  22. Porcine reproductive and respiratory syndrome virus field isolates differ in in vitro interferon phenotypes. Lee, S.M., Schommer, S.K., Kleiboeker, S.B. Vet. Immunol. Immunopathol. (2004) [Pubmed]
  23. Modulatory effect of mycobacterium cell wall extract (Regressin) on lymphocyte blastogenic activity and macrophage cytokine gene transcription in swine. Vézina, S.A., Archambault, D. Clin. Diagn. Lab. Immunol. (1997) [Pubmed]
  24. Hepatic sinusoidal endothelium upregulates IL-1alpha, IFN-gamma, and iNOS in response to discordant xenogeneic islets in an in vitro model of xenoislet transplantation. Tan, M., Di Carlo, A., Liu, S.Q., Tector, A.J., Tchervenkov, J.I., Metrakos, P. J. Surg. Res. (2002) [Pubmed]
  25. Transforming growth factor-beta 1 and -beta 2 positively regulate TGF-beta 1 mRNA expression in trabecular cells. Li, J., Tripathi, B.J., Chalam, K.V., Tripathi, R.C. Invest. Ophthalmol. Vis. Sci. (1996) [Pubmed]
  26. Kinetic evidence for a reversible isomerization of pig muscle glyceraldehyde-3-phosphate dehydrogenase in its crystallization medium. Vas, M., Berni, R., Batke, J., Keleti, T., Rossi, G.L. Arch. Biochem. Biophys. (1988) [Pubmed]
  27. Identification of the mammalian DNA-binding protein P8 as glyceraldehyde-3-phosphate dehydrogenase. Perucho, M., Salas, J., Salas, M.L. Eur. J. Biochem. (1977) [Pubmed]
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