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http://dx.doi.org/10.1007/s10059-009-0151-7

Glyceraldehyde-3-Phosphate, a Glycolytic Intermediate, Plays a Key Role in Controlling Cell Fate Via Inhibition of Caspase Activity  

Jang, Mi (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Kang, Hyo Jin (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology)
Lee, Sun Young (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Chung, Sang J. (BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology)
Kang, Sunghyun (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Chi, Seung Wook (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Cho, Sayeon (College of Pharmacy, Chung-Ang University)
Lee, Sang Chul (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Lee, Chong-Kil (Department of Pharmacy, Chungbuk National University)
Park, Byoung Chul (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Bae, Kwang-Hee (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Park, Sung Goo (Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology)
Publication Information
Molecules and Cells / v.28, no.6, 2009 , pp. 559-563 More about this Journal
Abstract
Glyceraldehyde-3-phosphate is a key intermediate in several central metabolic pathways of all organisms. Aldolase and glyceraldehyde-3-phosphate dehydrogenase are involved in the production or elimination of glyceraldehyde-3-phosphate during glycolysis or gluconeogenesis, and are differentially expressed under various physiological conditions, including cancer, hypoxia, and apoptosis. In this study, we examine the effects of glyceraldehyde-3-phosphate on cell survival and apoptosis. Overexpression of aldolase protected cells against apoptosis, and addition of glyceraldehyde-3-phosphate to cells delayed apoptosis. Additionally, delayed apoptotic phenomena were observed when glyceraldehyde-3-phosphate was added to a cell-free system, in which artificial apoptotic process was induced by adding dATP and cytochrome c. Surprisingly, glyceraldehyde-3-phosphate directly suppressed caspase-3 activity in a reversible noncompetitive mode, preventing caspase-dependent proteolysis. Based on these results, we suggest that glyceraldehyde-3-phosphate, a key molecule in several central metabolic pathways, functions as a molecule switch between cell survival and apoptosis.
Keywords
aldolase; apoptosis; caspase-3; GAPDH; glyceraldehyde-3-phosphate;
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Times Cited By Web Of Science : 6  (Related Records In Web of Science)
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1 Altenberg, B., and Greulich, K.O. (2004). Genes of glycolysis are ubiquitously overexpressed in 24 cancer classes. Genomics 84, 1014-1020   DOI   ScienceOn
2 Fang, B., Boross, P., Tozser, J., and Weber, I.T. (2006). Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition. J. Mol. Biol. 360, 654-666   DOI   ScienceOn
3 Jang, M., Park, B.C., Lee, A.Y., Na, K.S., Kang, S., Bae, K.-H., Myung, P.K., Chung, B.C., Cho, S., Lee, D.H., et al. (2007). Caspase-7 mediated cleavage of proteasome subunits during apoptosis. Biochem. Biophys. Res. Commun. 363, 388-394   DOI   ScienceOn
4 Jiang, X., and Wang, X. (2000). Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to apaf-1. J. Biol. Chem. 275, 31199-31203   DOI   ScienceOn
5 Lee, A.Y., Park, B.C., Jang, M., Cho, S., Lee, D.H., Lee, S.C., Myung, P.K., and Park, S.G. (2004). Identification of caspase-3 degradome by two-dimensional gel electrophoresis and matrixassisted laser desorption/ionization-time of flight analysis. Proteomics 4, 3429-3436   DOI   ScienceOn
6 Lu, H., Forbes, R.A., and Verma, A. (2002). Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis. J. Biol. Chem. 277, 23111-23115   DOI   ScienceOn
7 Priault, M., Chaudhuri, B., Clow, A., Camougrand, N., and Manon, S. (1999). Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement. Eur. J. Biochem. 260, 684-691   DOI   ScienceOn
8 Sen, N., Hara, M., Kornberg, M.D., Cascio, M.B., Bae, B.I., Shahani, N., Thomas, B., Dawson, T.M., Dawson, V.L., Snyder, S.H., et al. (2008). Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis. Nat. Cell Biol. 10, 866-873   DOI   ScienceOn
9 Shimizu, T., Kono, N., Kiyokawa, H., Yamada, Y., Hara, N., Mineo, I., Kawachi, M., Nakajima, H., Wang, Y.L., and Tarui, S. (1998). Erythrocyte glycolysis and its marked alteration by muscular exercise in type VII glycogenosis. Blood 71, 1130-1134
10 Segel, I.H. (1975). Enzyme kinetics, Chapter 7 and 8, (New York: Wiley.Inter.science)
11 Majors, B.S., Betenbaugh, M.J., and Chiang, G.G. (2007). Links between metabolism and apoptosis in mammalian cells: applications for anti-apoptosis engineering. Metab. Eng. 9, 317-326   DOI   ScienceOn
12 Chuang, D.-M., Hough, C., and Senatorov, V.V. (2005). Glyceraldehyde- 3-phosphate dehydrogenase, apoptosis, and neurodegenerative diseases. Annu. Rev. Pharmacol. Toxicol. 45, 269- 290   DOI   ScienceOn
13 Robey, R.B., and Hay, N. (2006). Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt. Oncogene 25, 4683-4696   DOI   ScienceOn
14 Ishitani, R., Sunaga, K., Hirano, A., Saunders, P., Katsube, N., Tanaka, M., and Chuang, D.M. (1996). Evidence that glyceraldehyde- 3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar granule neurons in culture. J. Neurochem. 66, 928-935   DOI   PUBMED   ScienceOn
15 Leist, M., Single, B., Castoldi, A.F., Kuhnle, S., and Nicotera, P. (1997). Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J. Exp. Med. 185, 1481-1486   DOI   ScienceOn
16 Li, C., Xiao, Z., Zhang, X., Li, J., Li, X., Yi, H., Li, M., Zhu, G., and Liang, S. (2006). Proteome analysis of human lung squamous carcinoma. Proteomics 6, 547-558   DOI   ScienceOn
17 Hoque, M.A., Ushiyama, H., Tomita, M., and Shimizu, K. (2005). Dynamic responses of the intracellular metabolite concentrations of the wild type and pkyA mutant Escherichia coli against pulse addition of glucose or $NH_3$ under those limiting continuous cultures. Biochem. Eng. 26, 38-49   DOI   ScienceOn
18 Jang, M., Park, B.C., Kang, S., Lee, D.H., Cho, S., Lee, S.C., Bae, K.-H., and Park, S.G. (2008). Mining of caspase-7 substrates using a degradomic approach. Mol. Cells 26, 152-157   PUBMED
19 Kumar, S. (2007). Caspase function in programmed cell death. Cell Death Differ. 14, 32-43   DOI   PUBMED   ScienceOn
20 Plas, D.R., and Thompson, C.B. (2002). Cell metabolism in the regulation of programmed cell death. Trends Endocrinol. Metab. 13, 75-78   DOI   ScienceOn
21 Vazquez, A., de Menezes, M.A., Barabasi, A.-L., and Oltvai, Z.N. (2008). Impact of limited solvent capacity on metabolic rate, enzyme activities, and metabolite concentrations of S. cerevisiae glycolysis. PloS Comp. Biol. 4, e1000195   DOI   ScienceOn
22 Jang, M., Park, B.C., Kang, S., Chi, S.-W., Cho, S., Chung, S.J., Lee, S.C., Bae, K.-H., and Park, S.G. (2009). Far upstream element- binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene. Oncogene 28, 1529-1536   DOI   ScienceOn
23 Kass, G.E., Eriksson, J.E., Weis, M., Orrenius, S., and Chow, S.C. (1996). Chromatin condensation during apoptosis requires ATP. Biochem. J. 318, 749-752   DOI
24 Vander Heiden, M.G., Plas, D.R., Rathmell, J.C., Fox, C.J., Harris, M.H., and Thompson, C.B. (2001). Growth factors can influence cell growth and survival though effects on glucose metabolism. Mol. Cell. Biol. 21, 5899-5912   DOI   ScienceOn
25 Shim, H.Y., Park, J.H., Paik, H.D., Nah, S.Y., Kim, D.S., and Han Y.S. (2007). Acacetin-induced apoptosis of human breast cancer MCF-7 cells involves caspase cascade, mitochondriamediated death signaling and SAPK/JNK1/2-c-Jun activation. Mol. Cells 24, 95-104   PUBMED
26 Unwin, R.D., Craven, R.A., Harnden, P., Hanrahan, S., Totty, N., Knowles, M., Eardley, I., Selby, P.J., and Banks, R.E. (2003). Proteomic changes in renal cancer and co-ordinate demonstration of both the glycolytic and mitochondrial aspects of the Warburg effect. Proteomics 3, 1620-1632   DOI   ScienceOn
27 Harlin, H., Reffey, S.B., Duckett, C.S., Lindsten, T., and Thompson, C.B. (2001). Characterization of XIAP-deficient mice. Mol. Cell. Biol. 21, 3604-3608   DOI   ScienceOn
28 Na, K.S., Park, B.C., Jang, M., Cho, S., Lee, D.H., Kang, S., Lee, C.-K., Bae, K.-H., and Park, S.G. (2007). Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis. Mol. Cells 24, 261-267   PUBMED
29 Adrain, C., Creagh, E.M., Cullen, S.P., and Martin, S.J. (2004). Caspase-dependent inactivation of proteasome function during programmed cell death in drosophila and man. J. Biol. Chem. 27, 36923-36930
30 Garland, J.M., and Halestrap, A. (1997). Energy metabolism during apoptosis. Bcl-2 promotes survival in hematopoietic cells induced to apoptose by growth factor withdrawal by stabilizing a form of metabolic arrest. J. Biol. Chem. 272, 4680-4688   DOI   ScienceOn
31 Bao, Q., and Shi, Y. (2007). Apoptosome: a platform for the activation of initiator caspases. Cell Death Differ. 14, 56-65   DOI   ScienceOn
32 Kilic, M., Kasperczyk, H., Fulda, S., and Debatin, K.-M. (2007). Role of hypoxia inducible factor-1 alpha in modulation of apoptosis resistance. Oncogene 26, 2027-2038   DOI   ScienceOn
33 Schaefer, U., Boos, W., Takors, R., and Weuster-Botz, D. (1999). Automated sampling device for monitoring intracellular metabolite dynamics. Anal. Biochem. 270, 88-96   DOI   ScienceOn