HIF-1-regulated glucose metabolism in the control of apoptosis signaling

References

• Semenza GL, Agani F, Feldser D et al. Hypoxia, HIF-1, and the pathophysiology of common human diseases. Adv. Exp. Med. Biol.475, 123–130 (2000).
   PubMed Web of Science ®Google Scholar
• Harris AL. Hypoxia – a key regulatory factor in tumour growth. Nat. Rev. Cancer2(1), 38–47 (2002).
   PubMed Web of Science ®Google Scholar
• Gordan JD, Simon MC. Hypoxia-inducible factors: central regulators of the tumor phenotype. Curr. Opin. Genet. Dev.17(1), 71–77 (2007).
   PubMed Web of Science ®Google Scholar
• Semenza G. Signal transduction to hypoxia-inducible factor 1. Biochem. Pharmacol.64(5–6), 993ndash;998 (2002).
   PubMed Web of Science ®Google Scholar
• Hirota K, Semenza GL. Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases. Biochem. Biophys. Res. Commun.338(1), 610–616 (2005).
   PubMed Web of Science ®Google Scholar
• Maxwell PH, Wiesener MS, Chang GW et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature399(6733), 271–275 (1999).
   PubMed Web of Science ®Google Scholar
• Huang LE, Gu J, Schau M, Bunn HF. Regulation of hypoxia-inducible factor 1α is mediated by an O2-dependent degradation domain via the ubiquitin–proteasome pathway. Proc. Natl Acad. Sci. USA95(14), 7987–7992 (1998).
   PubMed Web of Science ®Google Scholar
• Majumder PK, Febbo PG, Bikoff R et al. mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways. Nat. Med.10(6), 594–601 (2004).
   PubMed Web of Science ®Google Scholar
• Jiang BH, Jiang G, Zheng JZ, Lu Z, Hunter T, Vogt PK. Phosphatidylinositol 3-kinase signaling controls levels of hypoxia-inducible factor 1. Cell Growth Differ.12(7), 363–369 (2001).
   PubMedGoogle Scholar
• Cramer T, Yamanishi Y, Clausen BE et al. HIF-1α is essential for myeloid cell-mediated inflammation. Cell112(5), 645–657 (2003).
   PubMed Web of Science ®Google Scholar
• Isaacs JS, Jung YJ, Mole DR et al. HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability. Cancer Cell8(2), 143–153 (2005).
   PubMed Web of Science ®Google Scholar
• Pollard PJ, Spencer-Dene B, Shukla D et al. Targeted inactivation of fh1 causes proliferative renal cyst development and activation of the hypoxia pathway. Cancer Cell11(4), 311–319 (2007).
   PubMed Web of Science ®Google Scholar
• Semenza GL. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer3(10), 721–732 (2003).
   PubMed Web of Science ®Google Scholar
• Giaccia A, Siim BG, Johnson RS. HIF-1 as a target for drug development. Nat. Rev. Drug Discov.2(10), 803–811 (2003).
   PubMed Web of Science ®Google Scholar
• Zhong H, De Marzo AM, Laughner E et al. Overexpression of hypoxia-inducible factor 1α in common human cancers and their metastases. Cancer Res.59(22), 5830–5835 (1999).
   PubMed Web of Science ®Google Scholar
• Akakura N, Kobayashi M, Horiuchi I et al. Constitutive expression of hypoxia-inducible factor-1α renders pancreatic cancer cells resistant to apoptosis induced by hypoxia and nutrient deprivation. Cancer Res.61(17), 6548–6554 (2001).
   PubMed Web of Science ®Google Scholar
• Piret J-P, Lecocq C, Toffoli S, Ninane N, Raes M, Michiels C. Hypoxia and CoCl2 protect HepG2 cells against serum deprivation- and t-BHP-induced apoptosis: a possible anti-apoptotic role for HIF-1. Exp. Cell. Res.295(2), 340–349 (2004).
   Google Scholar
• Zhang Q, Zhang Z-F, Rao JY et al. Treatment with siRNA and antisense oligonucleotides targeted to HIF-1α induced apoptosis in human tongue squamous cell carcinomas. Int. J. Cancer111(6), 849–857 (2004).
   PubMed Web of Science ®Google Scholar
• Kim J-Y, Ahn H-J, Ryu J-H, Suk K, Park J-H. BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1α. J. Exp. Med.199(1), 113–124 (2004).
   PubMed Web of Science ®Google Scholar
• Kim M, Park S-Y, Pai H-S, Kim T-H, Billiar TR, Seol D-W. Hypoxia inhibits tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by blocking Bax translocation. Cancer Res.64(12), 4078–4081 (2004).
   PubMed Web of Science ®Google Scholar
• Dong Z, Wang JZ, Yu F, Venkatachalam MA. Apoptosis-resistance of hypoxic cells: multiple factors involved and a role for IAP-2. Am. J. Pathol.163(2), 663–671 (2003).
   PubMedGoogle Scholar
• Kilic M, Kasperczyk H, Fulda S, Debatin KM. Role of hypoxia inducible factor-1α in modulation of apoptosis resistance. Oncogene26(14), 2027–2038 (2007).
   PubMed Web of Science ®Google Scholar
• Erler JT, Cawthorne CJ, Williams KJ et al. Hypoxia-mediated down-regulation of Bid and Bax in tumors occurs via hypoxia-inducible factor 1-dependent and -independent mechanisms and contributes to drug resistance. Mol. Cell. Biol.24(7), 2875–2889 (2004).
   PubMed Web of Science ®Google Scholar
• Bacon AL, Harris AL. Hypoxia-inducible factors and hypoxic cell death in tumour physiology. Ann. Med.36(7), 530–539 (2004).
   PubMed Web of Science ®Google Scholar
• Greijer AE, van der Wall E. The role of hypoxia inducible factor 1 (HIF-1) in hypoxia induced apoptosis. J. Clin. Pathol.57(10), 1009–1014 (2004).
   PubMed Web of Science ®Google Scholar
• Carmeliet P, Dor Y, Herbert JM et al. Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis. Nature394(6692), 485–490 (1998).
   PubMed Web of Science ®Google Scholar
• Bruick RK. Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc. Natl Acad. Sci. USA97(16), 9082–9087 (2000).
   PubMed Web of Science ®Google Scholar
• Guo K, Searfoss G, Krolikowski D et al. Hypoxia induces the expression of the pro-apoptotic gene BNIP3. Cell Death Differ.8(4), 367–376 (2001).
   PubMed Web of Science ®Google Scholar
• Sowter HM, Ratcliffe PJ, Watson P, Greenberg AH, Harris AL. HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors. Cancer Res.61(18), 6669–6673 (2001).
   PubMed Web of Science ®Google Scholar
• Tracy K, Dibling BC, Spike BT, Knabb JR, Schumacker P, Macleod KF. BNIP3 is an RB/E2F target gene required for hypoxia-induced autophagy. Mol. Cell. Biol.27(17), 6229–6242 (2007).
   PubMed Web of Science ®Google Scholar
• Azad MB, Chen Y, Henson ES et al. Hypoxia induces autophagic cell death in apoptosis-competent cells through a mechanism involving BNIP3. Autophagy4(2), 195–204 (2008).
   PubMed Web of Science ®Google Scholar
• Zhang H, Bosch-Marce M, Shimoda LA et al. Mitochondrial autophagy is a HIF-1-dependent adaptive metabolic response to hypoxia. J. Biol. Chem.(2008) (Epub ahead of print).
   Google Scholar
• Maiuri MC, Zalckvar E, Kimchi A, Kroemer G. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat. Rev. Mol. Cell Biol.8(9), 741–752 (2007).
   PubMed Web of Science ®Google Scholar
• Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell132(1), 27–42 (2008).
   PubMed Web of Science ®Google Scholar
• Park S-Y, Billiar TR, Seol D-W. Hypoxia inhibition of apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand (TRAIL). Biochem. Biophys. Res. Commun.291(1), 150–153 (2002).
   PubMed Web of Science ®Google Scholar
• Mathupala SP, Rempel A, Pedersen PL. Glucose catabolism in cancer cells: identification and characterization of a marked activation response of the type II hexokinase gene to hypoxic conditions. J. Biol. Chem.276(46), 43407–43412 (2001).
   PubMed Web of Science ®Google Scholar
• Blum R, Jacob-Hirsch J, Amariglio N, Rechavi G, Kloog Y. Ras inhibition in glioblastoma down-regulates hypoxia-inducible factor-1α, causing glycolysis shutdown and cell death. Cancer Res.65(3), 999–1006 (2005).
   PubMed Web of Science ®Google Scholar
• Kim J-W, Dang CV. Cancer’s molecular sweet tooth and the Warburg effect. Cancer Res.66(18), 8927–8930 (2006).
   PubMed Web of Science ®Google Scholar
• Gatenby RA, Gillies RJ. Why do cancers have high aerobic glycolysis? Nat. Rev. Cancer4(11), 891–899 (2004).
   PubMed Web of Science ®Google Scholar
• Discher DJ, Bishopric NH, Wu X, Peterson CA, Webster KA. Hypoxia regulates β-enolase and pyruvate kinase-M promoters by modulating Sp1/Sp3 binding to a conserved GC element. J. Biol. Chem.273(40), 26087–26093 (1998).
   PubMed Web of Science ®Google Scholar
• Murphy BJ, Andrews GK, Bittel D et al. Activation of metallothionein gene expression by hypoxia involves metal response elements and metal transcription factor-1. Cancer Res.59(6), 1315–1322 (1999).
   PubMed Web of Science ®Google Scholar
• Hochachka PW, Lutz PL. Mechanism, origin, and evolution of anoxia tolerance in animals. Comp. Biochem. Physiol. B Biochem. Mol. Biol.130(4), 435–459 (2001).
   PubMed Web of Science ®Google Scholar
• Webster KA, Discher DJ, Hernandez OM, Yamashita K, Bishopric NH. A glycolytic pathway to apoptosis of hypoxic cardiac myocytes. Molecular pathways of increased acid production. Adv. Exp. Med. Biol.475, 161–175 (2000).
   Google Scholar
• Kim J-W, Tchernyshyov I, Semenza GL, Dang CV. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab.3(3), 177–185 (2006).
   PubMed Web of Science ®Google Scholar
• Papandreou I, Cairns RA, Fontana L, Lim AL, Denko NC. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab.3(3), 187–197 (2006).
   PubMed Web of Science ®Google Scholar
• Cairns RA, Papandreou I, Sutphin PD, Denko NC. Metabolic targeting of hypoxia and HIF1 in solid tumors can enhance cytotoxic chemotherapy. Proc. Natl Acad. Sci. USA104(22), 9445–9450 (2007).
   PubMed Web of Science ®Google Scholar
• Plas DR, Thompson CB. Cell metabolism in the regulation of programmed cell death. Trends Endocrinol. Metab.13(2), 75–78 (2002).
   PubMedGoogle Scholar
• Deberardinis RJ, Lum JJ, Hatzivassiliou G, Thompson CB. The biology of cancer: metabolic reprogramming fuels cell growth and proliferation. Cell Metab.7(1), 11–20 (2008).
   PubMed Web of Science ®Google Scholar
• Chen J, Zhao S, Nakada K et al. Dominant-negative hypoxia-inducible factor-1α reduces tumorigenicity of pancreatic cancer cells through the suppression of glucose metabolism. Am. J. Pathol.162(4), 1283–1291 (2003).
   PubMed Web of Science ®Google Scholar
• Lin Z, Weinberg JM, Malhotra R, Merritt SE, Holzman LB, Brosius FC 3rd. GLUT-1 reduces hypoxia-induced apoptosis and JNK pathway activation. Am. J. Physiol. Endocrinol. Metab.278(5), E958–E966 (2000).
   PubMed Web of Science ®Google Scholar
• Gottlob K, Majewski N, Kennedy S, Kandel E, Robey RB, Hay N. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev.15(11), 1406–1418 (2001).
   PubMed Web of Science ®Google Scholar
• Majewski N, Nogueira V, Bhaskar P et al. Hexokinase–mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak. Mol. Cell16(5), 819–830 (2004).
   PubMed Web of Science ®Google Scholar
• Pastorino JG, Hoek JB. Hexokinase II: the integration of energy metabolism and control of apoptosis. Curr. Med. Chem.10(16), 1535–1551 (2003).
   PubMed Web of Science ®Google Scholar
• Rathmell JC, Fox CJ, Plas DR, Hammerman PS, Cinalli RM, Thompson CB. Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival. Mol. Cell. Biol.23(20), 7315–7328 (2003).
   PubMed Web of Science ®Google Scholar
• Ishitani R, Chuang DM. Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons. Proc. Natl Acad. Sci. USA93(18), 9937–9941 (1996).
   PubMedGoogle Scholar
• Dastoor Z, Dreyer JL. Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress. J. Cell Sci.114(Pt 9), 1643–1653 (2001).
   PubMed Web of Science ®Google Scholar
• Shashidharan P, Chalmers-Redman RM, Carlile GW et al. Nuclear translocation of GAPDH–GFP fusion protein during apoptosis. Neuroreport10(5), 1149–1153 (1999).
   Google Scholar
• Colell A, Ricci J-E, Tait S et al. GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation. Cell129(5), 983–997 (2007).
   PubMed Web of Science ®Google Scholar
• Semenza GL. Evaluation of HIF-1 inhibitors as anticancer agents. Drug Discov. Today12(19–20), 853–859 (2007).
   PubMed Web of Science ®Google Scholar
• Melillo G. Targeting hypoxia cell signaling for cancer therapy. Cancer Metastasis Rev.26(2), 341–352 (2007).
   PubMed Web of Science ®Google Scholar
• Bjornsti M-A, Houghton PJ. The TOR pathway: a target for cancer therapy. Nat. Rev. Cancer4(5), 335–348 (2004).
   PubMed Web of Science ®Google Scholar
• Easton JB, Houghton PJ. mTOR and cancer therapy. Oncogene25(48), 6436–6446 (2006).
   PubMed Web of Science ®Google Scholar
• Faivre S, Kroemer G, Raymond E. Current development of mTOR inhibitors as anticancer agents. Nat. Rev. Drug Discov.5(8), 671–688 (2006).
   PubMed Web of Science ®Google Scholar
• Isaacs JS, Jung Y-J, Mimnaugh EG, Martinez A, Cuttitta F, Neckers LM. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway. J. Biol. Chem.277(33), 29936–29944 (2002).
   PubMed Web of Science ®Google Scholar
• Liu YV, Baek JH, Zhang H, Diez R, Cole RN, Semenza GL. RACK1 competes with HSP90 for binding to HIF-1α and is required for O2-independent and HSP90 inhibitor-induced degradation of HIF-1α. Mol. Cell25(2), 207–217 (2007).
   PubMed Web of Science ®Google Scholar
• Kaluz S, Kaluzova M, Stanbridge EJ. Proteasomal inhibition attenuates transcriptional activity of hypoxia-inducible factor 1 (HIF-1) via specific effect on the HIF-1α C-terminal activation domain. Mol. Cell. Biol.26(15), 5895–5907 (2006).
   PubMed Web of Science ®Google Scholar
• Fath DM, Kong X, Liang D et al. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-α. J. Biol. Chem.281(19), 13612–13619 (2006).
   PubMed Web of Science ®Google Scholar