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Gene Review

LOC291536  -  glyceraldehyde-3-phosphate dehydrogenase-like

Rattus norvegicus

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Disease relevance of LOC291536

  • GAPDH expression closely correlates with cell motility of Dunning prostate cancer cell lines and accurately distinguishes cell lines with high metastatic potential from those with low metastatic potential [1].
  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) expression is increased in Dunning R-3327 rat prostatic adenocarcinoma cell lines relative to normal rat ventral prostate tissue [1].
  • The authors' study demonstrated that overexpression of GAPDH and nuclear translocation occurred in both the ischemic core and penumbra area soon after focal ischemia [2].
  • The mean mRNA ratio of group II PLA2/GAPDH was increased in liver tissue by 126% (P < 0.001) and in kidney tissue by 263% (P < 0.006) following induction of liver cirrhosis [3].
  • The mean mRNA ratio of annexin-I/GAPDH was increased in liver tissue by 115% (P < 0.05) but unchanged in kidney tissue following induction of cirrhosis [3].

Psychiatry related information on LOC291536

  • These results raise the possibility that GAPDH is also involved in the neurodegeneration during the development of Alzheimer's disease [4].

High impact information on LOC291536


Chemical compound and disease context of LOC291536


Biological context of LOC291536

  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) influences cytotoxicity, translocating to the nucleus during apoptosis [5].
  • These combined results suggest that Rab2 stimulated PKCiota/lambda and GAPDH recruitment to VTCs, and the subsequent PKCiota/lambda phosphorylation of GAPDH ultimately influences MT dynamics in the early secretory pathway [13].
  • To determine whether GAPDH catalytic activity was critical for transport in the early secretory pathway, a conservative substitution was made at Cys-149 located at the active site, and the mutant was biochemically characterized in a battery of assays [14].
  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key regulatory enzyme of glycolysis, which exists in nuclei and functions as a DNA-binding protein as well as a nuclear protein, appears to be modulated by cellular activities [15].
  • Thus, the inhibition of PDGF-BB-induced expression of GAPDH by SB suggests a link between SMC proliferation, energy consumption, and GAPDH gene upregulation [15].

Anatomical context of LOC291536

  • Based on numerous observations that show (beta-COP) GAPDH associates with cytoskeletal elements, we examined the role of phospho-GAPDH in promoting microtubule (MT) binding to membrane [13].
  • Importantly, VSV-G transport between the ER and Golgi complex is restored when an in vitro trafficking assay is performed with GAPDH-depleted cytosol and GAPDH (C149G) [14].
  • We propose that membranes incubated with anti-GAPDH and Rab2 form "dead end" vesicles that are unable to transport and fuse with the acceptor compartment [16].
  • We have previously established that GAPDH is required for membrane transport between the endoplasmic reticulum and the Golgi complex [14].
  • Rab2-treated microsomes showed a 5-10-fold increase in the level of membrane-associated GAPDH [16].

Associations of LOC291536 with chemical compounds

  • Prior to AraC-induced neuronal death, GAPDH mRNA levels increased by approximately 2.5-fold, and this mRNA accumulation was blocked by actinomycin-D and the GAPDH antisense (but not sense) oligonucleotide [17].
  • The reduction in PDGF-BB-induced GAPDH expression by SB is probably caused by a cycloheximide-insensitive transcriptional mechanism [15].
  • Treatment with growth hormone and alcohol show no disparity in GAPDH mRNA levels whereas in some experiments, parathyroid hormone and 17beta-estradiol increased GAPDH mRNA levels [18].
  • Co-operation was elucidated between norepinephrine- and insulin-mediated induction of GAPDH mRNA levels [19].
  • We therefore surmised that the cysteine residues of GAPDH react with ferrylMb [20].

Other interactions of LOC291536

  • Renin qRTPCR in ANG II-infused rats showed higher mRNA levels in the kidney medulla compared with sham-operated rats (5.5 +/- 2.3 vs. 0.04 +/- 0.02 ratio to GAPDH mRNA levels; P < 0.001); however, renin transcript levels were normalized in the ARB-treated rats [21].
  • Relative to GAPDH mRNA levels and compared with untreated neurons, NMDA increased exon 3-specific BDNF mRNA twofold [22].
  • Kidney VDR mRNA relative to GAPDH mRNA correlated inversely with serum 1,25(OH)(2)D (r = -0.714, P = 0.006) [23].
  • Staurosporine (64 nM) and TPA (49 nM) enhanced the level of CINC-3 mRNA time-dependently, but had no effect on GAPDH mRNA levels [24].
  • Fudenine, a C-terminal truncated rat homologue of mouse prominin, is blood glucose-regulated and can up-regulate the expression of GAPDH [25].

Analytical, diagnostic and therapeutic context of LOC291536

  • During the subsequent reperfusion, nuclear accumulation of GAPDH in this area decreased in a time-dependent manner [2].
  • Moreover, double staining revealed colocalization of nuclear GAPDH and TUNEL in the penumbra area [2].
  • This apparent discrepancy was partially resolved by the finding that rabbit muscle GAPDH could be fractionated into two components by affinity chromatography on single-stranded DNA cellulose [26].
  • CONCLUSIONS: In summary, this study indicates that nitric oxide generated during ischemic preconditioning could act as a glycolytic modulator during subsequent ischemia, through its effect on GAPDH activity [27].
  • Northern blot analysis showed that GAPDH mRNA levels increased during differentiation of precursor cells into mature adipocytes, mainly in the initial stages of the differentiation process [19].


  1. Association of glyceraldehyde-3-phosphate dehydrogenase expression with cell motility and metastatic potential of rat prostatic adenocarcinoma. Epner, D.E., Partin, A.W., Schalken, J.A., Isaacs, J.T., Coffey, D.S. Cancer Res. (1993) [Pubmed]
  2. Induction of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) expression in rat brain after focal ischemia/reperfusion. Tanaka, R., Mochizuki, H., Suzuki, A., Katsube, N., Ishitani, R., Mizuno, Y., Urabe, T. J. Cereb. Blood Flow Metab. (2002) [Pubmed]
  3. Liver cirrhosis induces renal and liver phospholipase A2 activity in rats. Vishwanath, B.S., Frey, F.J., Escher, G., Reichen, J., Frey, B.M. J. Clin. Invest. (1996) [Pubmed]
  4. Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain. Sunaga, K., Takahashi, H., Chuang, D.M., Ishitani, R. Neurosci. Lett. (1995) [Pubmed]
  5. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Hara, M.R., Agrawal, N., Kim, S.F., Cascio, M.B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J.H., Tankou, S.K., Hester, L.D., Ferris, C.D., Hayward, S.D., Snyder, S.H., Sawa, A. Nat. Cell Biol. (2005) [Pubmed]
  6. Regulation of transforming growth factor expression in rat intestinal epithelial cell lines. Suemori, S., Ciacci, C., Podolsky, D.K. J. Clin. Invest. (1991) [Pubmed]
  7. Inositol 1,4,5-trisphosphate receptor/GAPDH complex augments Ca2+ release via locally derived NADH. Patterson, R.L., van Rossum, D.B., Kaplin, A.I., Barrow, R.K., Snyder, S.H. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  8. Maternal diabetes in vivo and high glucose in vitro diminish GAPDH activity in rat embryos. Wentzel, P., Ejdesjö, A., Eriksson, U.J. Diabetes (2003) [Pubmed]
  9. Histone deacetylase inhibitor 4-phenylbutyrate suppresses GAPDH mRNA expression in glioma cells. Appelskog, I.B., Ammerpohl, O., Svechnikova, I.G., Lui, W.O., Almqvist, P.M., Ekström, T.J. Int. J. Oncol. (2004) [Pubmed]
  10. Effect of acrylamide and related compounds on glycolytic enzymes in rat sciatic nerve in vivo. Sakamoto, J., Hashimoto, K. Arch. Toxicol. (1985) [Pubmed]
  11. Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion. Eaton, P., Wright, N., Hearse, D.J., Shattock, M.J. J. Mol. Cell. Cardiol. (2002) [Pubmed]
  12. Quantitative polymerase chain reaction using an external control mRNA for determination of gene expression in a heterogeneous cell population. Shibata, M., Hariya, T., Hatao, M., Ashikaga, T., Ichikawa, H. Toxicol. Sci. (1999) [Pubmed]
  13. Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway. Tisdale, E.J. J. Biol. Chem. (2002) [Pubmed]
  14. Glyceraldehyde-3-phosphate dehydrogenase interacts with Rab2 and plays an essential role in endoplasmic reticulum to Golgi transport exclusive of its glycolytic activity. Tisdale, E.J., Kelly, C., Artalejo, C.R. J. Biol. Chem. (2004) [Pubmed]
  15. Inhibition of platelet-derived growth factor BB-induced expression of glyceraldehyde-3-phosphate dehydrogenase by sodium butyrate in rat vascular smooth muscle cells. Ranganna, K., Yatsu, F.M. Arterioscler. Thromb. Vasc. Biol. (1997) [Pubmed]
  16. Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway. Tisdale, E.J. J. Biol. Chem. (2001) [Pubmed]
  17. Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons. Ishitani, R., Chuang, D.M. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  18. Unanticipated changes in steady-state mRNA levels for glyceraldehyde-3-phosphate dehydrogenase in rat tibiae. Maran, A., Hefferan, T.E., Zhang, M., Turner, R.T. Calcif. Tissue Int. (2004) [Pubmed]
  19. Norepinephrine, tri-iodothyronine and insulin upregulate glyceraldehyde-3-phosphate dehydrogenase mRNA during Brown adipocyte differentiation. Barroso, I., Benito, B., Garcí-Jiménez, C., Hernández, A., Obregón, M.J., Santisteban, P. Eur. J. Endocrinol. (1999) [Pubmed]
  20. Inactivation of glyceraldehyde-3-phosphate dehydrogenase by ferrylmyoglobin. Miura, T., Muraoka, S., Ogiso, T. Chem. Biol. Interact. (1997) [Pubmed]
  21. AT1 receptor-mediated enhancement of collecting duct renin in angiotensin II-dependent hypertensive rats. Prieto-Carrasquero, M.C., Kobori, H., Ozawa, Y., Gutiérrez, A., Seth, D., Navar, L.G. Am. J. Physiol. Renal Physiol. (2005) [Pubmed]
  22. Nuclear factor kappaB is a critical determinant in N-methyl-D-aspartate receptor-mediated neuroprotection. Lipsky, R.H., Xu, K., Zhu, D., Kelly, C., Terhakopian, A., Novelli, A., Marini, A.M. J. Neurochem. (2001) [Pubmed]
  23. Improved cholecalciferol nutrition in rats is noncalcemic, suppresses parathyroid hormone and increases responsiveness to 1, 25-dihydroxycholecalciferol. Vieth, R., Milojevic, S., Peltekova, V. J. Nutr. (2000) [Pubmed]
  24. Induction of neutrophil chemotactic factor production by staurosporine in rat peritoneal neutrophils. Edamatsu, T., Xiao, Y.Q., Tanabe, J., Mue, S., Ohuchi, K. Br. J. Pharmacol. (1997) [Pubmed]
  25. Fudenine, a C-terminal truncated rat homologue of mouse prominin, is blood glucose-regulated and can up-regulate the expression of GAPDH. Zhu, G., Chang, Y., Zuo, J., Dong, X., Zhang, M., Hu, G., Fang, F. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  26. Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. Morgenegg, G., Winkler, G.C., Hübscher, U., Heizmann, C.W., Mous, J., Kuenzle, C.C. J. Neurochem. (1986) [Pubmed]
  27. Modification of glyceraldehyde-3-phosphate dehydrogenase in response to nitric oxide in intestinal preconditioning. Sola, A., Roselló-Catafau, J., Alfaro, V., Pesquero, J., Palacios, L., Gelpí, E., Hotter, G. Transplantation (1999) [Pubmed]
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