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Gene Review

GAPDH  -  glyceraldehyde-3-phosphate dehydrogenase

Gallus gallus

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Disease relevance of GAPDH

  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from chicken was expressed in and purified from Escherichia coli [1].
  • A yeast EcoRI fragment library in bacteriophage lambda was screened using the chicken cDNA plasmid as probe, and two recombinant phages were isolated, each one containing a different GAPDH gene [2].

High impact information on GAPDH

  • Sequencing of the chicken GAPDH gene revealed 11 introns [3].
  • Only one gene coding for glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC, a key enzyme in the control of glycolysis, is known to be functional in man, mouse, rat and chicken [4].
  • Comparison of nucleotide sequences indicates that the divergence of chloroplast and cytosolic GAPDH genes preceded the divergence of prokaryotes and eukaryotes [5].
  • The GAPDH coding region was detected within a 4.65-kilobase Xho I/EcoRI genomic fragment that was completely sequenced by using the M13 cloning vector system [6].
  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), an evolutionarily conserved glycolytic enzyme, is constitutively expressed in most cell types yet is induced to high levels during the development of fast twitch muscle fibers [6].

Biological context of GAPDH


Anatomical context of GAPDH


Associations of GAPDH with chemical compounds

  • Three proteins recognized by these antibodies were identified by partial amino acid sequencing to be glyceraldehyde-3-phosphate dehydrogenase (GAPDH), fructose-1,6-bisphosphate aldolase, and the regulator of chromatin condensation 1 [7].
  • Antisera raised against purified chicken GAPDH reacted with a 36K protein present in chick brain extracts and estimated to be the fourth most prevalent protein, as determined by either Coomassie Blue staining or by in vitro translation of chick brain mRNA [8].
  • Our current data on GAPDH provides an important link in this complex network of molecular changes involving pathways identified by our group and others, such as nitric oxide (NO), CaM kinase-II (CaMK-II), protein kinase-A (PKA), c-fos, and phosphorylated-CREB (p-CREB) in DFP-induced OPIDN [13].
  • MATERIALS AND METHODS: In the present study, we investigated mRNA levels of alpha 1(I), alpha 2(I), alpha 1(II), alpha 1(III), alpha 1(VI), alpha 2(VI), and alpha 3(VI) procollagen and GAPDH using digoxigenin-labeled antisense probes in a nonradioactive ribonuclease protection assay (RPA) [14].
  • Immunocomplex kinase assays indicated strong autophosphorylation of p51tkl at tyrosine residues and phosphorylation of exogenous substrates such as D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH), histones H2b and H4, and casein [15].

Regulatory relationships of GAPDH

  • Of these constant expressed genes, 28S rRNA and 18S rRNA are highly expressed; beta-actin intermediately expressed and GAPDH had a lower expression level in CE cell cultures [16].

Other interactions of GAPDH

  • Using semi-quantitative RT-PCR, expression of aggrecan, this chick CD44 orthologue and GAPDH mRNA was analyzed [11].
  • The levels of expression of mRNA for GAPDH, TGF-beta 1 and TGF-beta 2 were similar in the two groups, but the expression of TGF-beta 3 mRNA was significantly reduced in the samples from the dyschondroplastic growth plates [17].
  • Total RNA was extracted from cerebrum, cerebellum, brainstem, midbrain, and spinal cord of the control and DFP-treated hens, and northern blots were prepared using standard protocols and hybridized with GAPDH, as well as beta-actin and 28S RNA cDNA (control) probes [13].
  • Though no general pattern of enzyme activities in different species is discernible, high activities of TPI followed, in decreasing order, by GAPDH, enolase, PK, LDH and aldolase appear to be more common [18].
  • Real-time quantitative PCR was used to quantify pituitary expression of mRNAs encoding betaglycan, activin receptor (ActR) subtypes (type I, IIA), GnRH receptor (GnRH-R), LH beta subunit, FSH beta subunit and GAPDH [19].

Analytical, diagnostic and therapeutic context of GAPDH


  1. Glycine to alanine substitutions in helices of glyceraldehyde-3-phosphate dehydrogenase: effects on stability. Ganter, C., Plückthun, A. Biochemistry (1990) [Pubmed]
  2. Transcriptional mapping of two yeast genes coding for glyceraldehyde 3-phosphate dehydrogenase isolated by sequence homology with the chicken gene. Musti, A.M., Zehner, Z., Bostian, K.A., Paterson, B.M., Kramer, R.A. Gene (1983) [Pubmed]
  3. Intron-dependent evolution of chicken glyceraldehyde phosphate dehydrogenase gene. Stone, E.M., Rothblum, K.N., Schwartz, R.J. Nature (1985) [Pubmed]
  4. Unusual abundance of vertebrate 3-phosphate dehydrogenase pseudogenes. Piechaczyk, M., Blanchard, J.M., Riaad-El Sabouty, S., Dani, C., Marty, L., Jeanteur, P. Nature (1984) [Pubmed]
  5. Intron existence predated the divergence of eukaryotes and prokaryotes. Shih, M.C., Heinrich, P., Goodman, H.M. Science (1988) [Pubmed]
  6. Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene. Stone, E.M., Rothblum, K.N., Alevy, M.C., Kuo, T.M., Schwartz, R.J. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  7. Participation of a fusogenic protein, glyceraldehyde-3-phosphate dehydrogenase, in nuclear membrane assembly. Nakagawa, T., Hirano, Y., Inomata, A., Yokota, S., Miyachi, K., Kaneda, M., Umeda, M., Furukawa, K., Omata, S., Horigome, T. J. Biol. Chem. (2003) [Pubmed]
  8. Glyceraldehyde 3-phosphate dehydrogenase protein and mRNA are both differentially expressed in adult chickens but not chick embryos. Milner, R.J., Brow, M.D., Cleveland, D.W., Shinnick, T.M., Sutcliffe, J.G. Nucleic Acids Res. (1983) [Pubmed]
  9. Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis. Mezquita, J., Pau, M., Mezquita, C. J. Cell. Biochem. (1998) [Pubmed]
  10. Cloning, partial sequencing, and expression of glyceraldehyde-3-phosphate dehydrogenase gene in chick embryonic heart muscle cells. Arnold, H.H., Domdey, H., Wiebauer, K., Datta, K., Siddiqui, M.A. J. Biol. Chem. (1982) [Pubmed]
  11. Temporal expression of CD44 during embryonic chick limb development and modulation of its expression with retinoic acid. Rousche, K.T., Knudson, C.B. Matrix Biol. (2002) [Pubmed]
  12. Comparison on collagen gene expression in the developing chick embryo tendon and heart. Tissue and development time-dependent action of dexamethasone. Oikarinen, A., Mäkelä, J., Vuorio, T., Vuorio, E. Biochim. Biophys. Acta (1991) [Pubmed]
  13. Differential alteration of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mRNA in the central nervous system of hens treated with diisopropylphosphorofluoridate (DFP). Damodaran, T.V., Abdel-Rahman, A., El-Sourady, M.H., Abou-Donia, M.B. Neurochem. Int. (2002) [Pubmed]
  14. Altered procollagen mRNA expression during the progression of avian scleroderma. Ausserlechner, M.J., Sgonc, R., Dietrich, H., Wick, G. Mol. Med. (1997) [Pubmed]
  15. A strong protein-tyrosine kinase activity is associated with a baculovirus-expressed chicken tkl gene. Gärtner, T., Kühnel, H., Raab, G., Raab, M., Strebhardt, K., Rübsamen-Waigmann, H. Eur. J. Biochem. (1992) [Pubmed]
  16. Evaluation of the suitability of six host genes as internal control in real-time RT-PCR assays in chicken embryo cell cultures infected with infectious bursal disease virus. Li, Y.P., Bang, D.D., Handberg, K.J., Jorgensen, P.H., Zhang, M.F. Vet. Microbiol. (2005) [Pubmed]
  17. Expression of the gene for transforming growth factor-beta in avian dyschondroplasia. Law, A.S., Burt, D.W., Alexander, I., Thorp, B.H. Res. Vet. Sci. (1996) [Pubmed]
  18. Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order. Mathur, R.L., Reddy, M.C., Yee, S., Imbesi, R., Groth-Vasselli, B., Farnsworth, P.N. Exp. Eye Res. (1992) [Pubmed]
  19. Variation in pituitary expression of mRNAs encoding the putative inhibin co-receptor (betaglycan) and type-I and type-II activin receptors during the chicken ovulatory cycle. Lovell, T.M., Knight, P.G., Gladwell, R.T. J. Endocrinol. (2005) [Pubmed]
  20. Sequence analysis of the cloned mRNA coding for glyceraldehyde-3-phosphate dehydrogenase from chicken heart muscle. Domdey, H., Wiebauer, K., Klapthor, H., Arnold, H.H. Eur. J. Biochem. (1983) [Pubmed]
  21. Tail-to-head arrangement of a partial chicken glyceraldehyde-3-phosphate dehydrogenase processed pseudogene. Lum, R., Linial, M.L. J. Mol. Evol. (1997) [Pubmed]
  22. Cotransport of glyceraldehyde-3-phosphate dehydrogenase and actin in axons of chicken motoneurons. Yuan, A., Mills, R.G., Bamburg, J.R., Bray, J.J. Cell. Mol. Neurobiol. (1999) [Pubmed]
  23. Microcompartmentation of glycolytic enzymes in cultured cells. Minaschek, G., Gröschel-Stewart, U., Blum, S., Bereiter-Hahn, J. Eur. J. Cell Biol. (1992) [Pubmed]
  24. Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene. Ercolani, L., Florence, B., Denaro, M., Alexander, M. J. Biol. Chem. (1988) [Pubmed]
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