d? And how is it regulated? Is it carried out by a single form of GAPDH or it results from the induction of different isoforms?

This could help to develop a gene therapy with antisense oligodeoxynucleotides directed against the mRNA isoform (s) in cancer cases involving overexpression of GAPDH.


Our study has shown that in the three organs studied: Cervix, Breast and Prostate, GAPDH showed an overexpression in malignant tumor tissues. It has been shown that labeling was essentially nuclear in malignant lesions.

These results suggest GAPDH involvement in cancer process and draw attention to a probable new nuclear role. In addition to other functions already described such as its implication in glycolysis, apoptosis or oxidative stress, GAPDH may be implicated in DNA replication or repair.

Although GAPDH seems to be involved in malignant tumor process, there is no certainty about its specific role in the studied pathologies. Therefore it would be very interesting to evaluate the expression of the gene encoding this enzyme.

Moreover, it seems important to demonstrate whether the new role of GAPDH remains specific to a single form, or it is related to different isoforms of the enzyme, which can help to develop a gene therapy with antisense oligodeoxynucleotides directed against isoform(s) mRNA(s) in cases of cancer involving overexpression of GAPDH.


  1. Sygusch, J., Azema, L. and Dax, C. (2006) A first weapon against cancer metastases. Univalor Journal, 1, 1-2.
  2. Warburg, O.H. (1956) On the origin of cancer cells. Science, 123, 309-314. doi:10.1126/science.123.3191.309
  3. Soukri, A., Valverde, F., Hafid, N., Elkebbaj, M.S. and Serrano, A. (1996) Occurrence of a differential expression of the glyceraldehyde-3-phosphate dehydrogenase gene in muscle and liver from euthermic and induced hibernating jerboa (Jaculus orientalis). Gene Journal, 181, 139-145. doi:10.1016/S0378-1119(96)00494-5
  4. Iddar, A., Valverde, F., Serrano, A. and Soukri, A. (2002) Expression, purification and characterization of recombinant non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Clostridium acetobutylicum. Journal of Protein Expression and Purification, 25, 519-526. doi:10.1016/S1046-5928(02)00032-3
  5. Fothergill-Gilmore, L.A. and Pam, M. (1993) Evolution of Glycolysis. Journal of Progress in Biophysics and Molecular Biology, 95, 105-135. doi:10.1016/0079-6107(93)90001-Z
  6. Figge, R.M., Schubert, M., Brinkman, H. and Cerff, R. (1999) Glyceraldehyde phosphate dehydrogenase gene diversity in eubacteria an eukaryotes: Evidence for intraand inter-kingdom gene transfer. Journal of Molecular Biology and Evolution, 16, 429-440. doi:10.1093/oxfordjournals.molbev.a026125
  7. Habenicht, A. (1997) The non-phosphorylating glyceroldehyde-3-phosphate dehydrogenase: Biochemistry, structure, occurrence and evolution. Journal of Biological Chemistry, 378, 1413-1419.
  8. Bruns, G.A.P. and Gerald, P.S. (1976) Human glyceroldehyde-3-phosphate dehydrogenase in man-rodent somatic cell hybrids. Science, 192, 54-56. doi:10.1126/science.176725
  9. Sirover, M.A. (1999) New insights into an old protein: The functional diversity of mammalian glyceraldehyde- 3-phosphate dehydrogenase. Journal of Biochimica and Biophysica Acta, 1432, 159-184. doi:10.1016/S0167-4838(99)00119-3
  10. Barbini, L., Rodríguez, J., Dominguez, F. and Vega, F. (2007) Glyceraldehyde-3-phosphate dehydrogenase exerts different biologic activities in apoptotic and proliferating hepatocytes according to its subcellular localization. Journal of Molecular and Cellular Biochemistry, 300, 19- 28. doi:10.1007/s11010-006-9341-1
  11. Sirover, M.A. (2005) New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Journal of Cellular Biochemistry, 95, 45-52. doi:10.1002/jcb.20399
  12. Pitot, H.C. (1986) The biochemistry of neoplasia in vivo. Fundamentals of Oncology, Marcel Dekker, New York, 323-346.
  13. Zhou, Y.Y.X, Stoffer, B.J., Bonafe. N., Gilmore-Hebert, M., McAlpine, M. and Chambers, S.K. (2008) The multifunctional protein glyceraldehyde-3-phosphate dehydrogenase is both regulated and controls colony-stimulating factor-1 messenger RNA Stability in Ovarian Cancer. Journal of Molecular Cancer Research, 6, 1375- 1384. doi:10.1158/1541-7786.MCR-07-2170
  14. Du, Z.-X., Wang, H.Q., Zhang, H.Y. and Gao, D.X. (2007) Involvement of glyceraldehyde-3-phosphate dehydrogenase in tumor necrosis factor-related apoptosisinducing ligand-mediated death of thyroid cancer cells. Journal of endocrinology, 148, 4352. doi:10.1210/en.2006-1511
  15. Laffargue, F., Dargent, D. and Piana, L. (2002) Contribution des Sociétés françaises de chirurgie d’organe. Bulletin du Cancer, 89, 52-54.
  16. Parkin, D.M., Bray, F.I. and Devesa, S.S. (2001) Cancer burden in the year 2000 the global picture. Journal of European Journal of Cancer, 3, 4-66.
  17. Mountassif, D., Baibai, T., Fourrat, F., Moutaouakkil, A., Iddar, A., El Kebbaj, M.S. and Soukri, A. (2009) Immunoaffinity purification and characterization of Glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. Journal of Acta Biochimica & Biophysica Sinica, 41, 309-406.
  18. Pederson, P.L. (1978). Tumor mitochondria and the bioenergetics of cancer cells. Journal of Progress in Experimental Tumor Research, 22, 198-274.
  19. Epner, D.E., Partin, A.W., Schalken, J.A., Isaacs, J.T. and Coffey, D.S. (1993) Association of glyceraldehyde-3- phosphate dehydrogenase expression with cell motility and metastatic potential of rat prostatic adenocarcinoma. Journal of Cancer Research, 53, 1995-1997.
  20. Kim, J.W., Kim, S.J., Han, S.M., Paik, S.Y., Hur, S.Y., Kim, Y.W., Lee, J.M. and Namkoong, S.E. (1998) Increased glyceraldehyde-3-phosphate dehydrogenase gene expression in human cervical cancers. Journal of Gynecologic Oncology, 71, 266-269. doi:10.1006/gyno.1998.5195
  21. Correa, C.R., Bertollo, C.M., Zouain, C.S. and Goes A.M. (2010) Glyceraldehyde-3-phosphate dehydrogenase as an associated antigen on human breast cancer cell lines MACL-1 and MGSO-3. Journal of Oncology Reports, 24, 677-685.
  22. Kim, J.W., Kim, T.E., Kim, Y.K., Kim, Y.W., Kim, S.J., Lee, J.M., Kim, I.K. and Namkoong, S.E. (1999) Antisense oligodeoxynucleotide of glyceraldehyde-3-phosphate dehydrogenase gene inhibits cell proliferation and induces apoptosis in human cervical carcinoma cell lines. Journal of Antisense & Nucleic Acid Drug Development, 9, 507-513. doi:10.1089/oli.1.1999.9.507
  23. Shan, L., Xiang, G., Hoestje, S. and Epner, D.E. (2002) Identification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter. Journal of Biochimica and Biophysica Acta (BBA)—Gene Structure and Expression, 1574, 2152- 2156.
  24. Sirover, M.A. (1990) Cell cycle regulation of DNA repair enzymes and pathways. In: Milo, G.E. and Casto, B.C., Eds., Transformation of Human Diploid Fibroblasts, CRC Press, Boca Raton, 29-55.

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