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Volumn 20, Issue 1, 2010, Pages 51-56

HIF-1: upstream and downstream of cancer metabolism

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; GLUCOSE TRANSPORTER; GLYCOLYTIC ENZYME; HYPOXIA INDUCIBLE FACTOR 1; LACTIC ACID; PROTEIN BNIP3; PYRUVATE DEHYDROGENASE COMPLEX; PYRUVIC ACID;

EID: 76049100577     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2009.10.009     Document Type: Review
Times cited : (1103)

References (47)
  • 1
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • Gatenby R.A., and Gillies RJ. Why do cancers have high aerobic glycolysis?. Nat Rev Cancer 4 (2004) 891-899
    • (2004) Nat Rev Cancer , vol.4 , pp. 891-899
    • Gatenby, R.A.1    Gillies, RJ.2
  • 2
    • 1642565876 scopus 로고    scopus 로고
    • Tumor hypoxia and malignant progression
    • Vaupel P., Mayer A., and Hockel M. Tumor hypoxia and malignant progression. Methods Enzymol 381 (2004) 335-354
    • (2004) Methods Enzymol , vol.381 , pp. 335-354
    • Vaupel, P.1    Mayer, A.2    Hockel, M.3
  • 3
    • 67650531089 scopus 로고    scopus 로고
    • Genome-wide association of hypoxia-inducible factor (HIF)-1α and HIF-2α DNA binding with expression profiling of hypoxia-inducible transcripts
    • •] performed ChIP-chip (chromatin immunoprecipitation and mRNA microarray) analysis to identify direct target genes of HIF-1 and HIF-2. The majority of hypoxia-induced genes contained HIF-1 binding sites and expression was dependent on HIF-1α expression. HIF-2α bound to many of the same genes, but knockdown of HIF-2α levels did not affect gene expression. Hypoxia-repressed gene expression was also HIF-1α-dependent but did not involve direct HIF-1α binding to target genes.
    • •] performed ChIP-chip (chromatin immunoprecipitation and mRNA microarray) analysis to identify direct target genes of HIF-1 and HIF-2. The majority of hypoxia-induced genes contained HIF-1 binding sites and expression was dependent on HIF-1α expression. HIF-2α bound to many of the same genes, but knockdown of HIF-2α levels did not affect gene expression. Hypoxia-repressed gene expression was also HIF-1α-dependent but did not involve direct HIF-1α binding to target genes.
    • (2009) J Biol Chem , vol.284 , pp. 16767-16775
    • Mole, D.R.1    Blancher, C.2    Copley, R.R.3    Pollard, P.J.4    Gleadle, J.M.5    Ragoussis, J.6    Ratcliffe, P.J.7
  • 5
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • in press
    • Semenza GL: Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics. Oncogene, in press.
    • Oncogene
    • Semenza, G.L.1
  • 7
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin Jr. W.G., and Ratcliffe P.J. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol Cell 30 (2008) 393-402
    • (2008) Mol Cell , vol.30 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 8
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia
    • Guzy R.D., and Schumacker P.T. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 91 (2006) 807-819
    • (2006) Exp Physiol , vol.91 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 10
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden M.G., Cantley L.C., and Thompson C.B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324 (2009) 1029-1033
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 11
    • 33646917296 scopus 로고    scopus 로고
    • The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by hypoxia through a HIF-1α-dependent mechanism
    • Ullah M.S., Davies A.J., and Halestrap A.P. The plasma membrane lactate transporter MCT4, but not MCT1, is up-regulated by hypoxia through a HIF-1α-dependent mechanism. J Biol Chem 281 (2006) 9030-9037
    • (2006) J Biol Chem , vol.281 , pp. 9030-9037
    • Ullah, M.S.1    Davies, A.J.2    Halestrap, A.P.3
  • 12
    • 57449097020 scopus 로고    scopus 로고
    • Targeting lactate-fueled respiration selectively kills hypoxic tumor cells in mice
    • Tumors contain highly oxygenated (aerobic) and poorly oxygenated (hypoxic) regions, which were thought to utilize glucose for oxidative and glycolytic metabolism, respectively. Sonveaux et al. show that human cancer cells cultured under hypoxic conditions convert glucose to lactate and extrude it (via MCT4), whereas aerobic cancer cells take up lactate (via MCT1) and utilize it for oxidative phosphorylation. When MCT1 is inhibited, aerobic cancer cells take up glucose rather than lactate, and hypoxic cancer cells die as a result of glucose deprivation. Treatment of tumor-bearing mice with an inhibitor of MCT1 retarded tumor growth. MCT1 expression was detected exclusively in non-hypoxic regions of human cancer biopsy samples, and in combination, these data suggest that MCT1 inhibition holds potential as a novel cancer therapy.
    • Sonveaux P., Végran F., Schroeder T., Wergin M.C., Verrax J., Rabbani Z.N., De Saedeleer C.J., Kennedy K.M., Diepart C., Jordan B.F., et al. Targeting lactate-fueled respiration selectively kills hypoxic tumor cells in mice. J Clin Invest 118 (2008) 3930-3942. Tumors contain highly oxygenated (aerobic) and poorly oxygenated (hypoxic) regions, which were thought to utilize glucose for oxidative and glycolytic metabolism, respectively. Sonveaux et al. show that human cancer cells cultured under hypoxic conditions convert glucose to lactate and extrude it (via MCT4), whereas aerobic cancer cells take up lactate (via MCT1) and utilize it for oxidative phosphorylation. When MCT1 is inhibited, aerobic cancer cells take up glucose rather than lactate, and hypoxic cancer cells die as a result of glucose deprivation. Treatment of tumor-bearing mice with an inhibitor of MCT1 retarded tumor growth. MCT1 expression was detected exclusively in non-hypoxic regions of human cancer biopsy samples, and in combination, these data suggest that MCT1 inhibition holds potential as a novel cancer therapy.
    • (2008) J Clin Invest , vol.118 , pp. 3930-3942
    • Sonveaux, P.1    Végran, F.2    Schroeder, T.3    Wergin, M.C.4    Verrax, J.5    Rabbani, Z.N.6    De Saedeleer, C.J.7    Kennedy, K.M.8    Diepart, C.9    Jordan, B.F.10
  • 13
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia
    • Kim J.W., Tchernyshyov I., Semenza G.L., and Dang C.V. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab 3 (2006) 177-185
    • (2006) Cell Metab , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 14
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I., Cairns R.A., Fontana L., Lim A.L., and Denko N.C. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab 3 (2006) 187-197
    • (2006) Cell Metab , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 15
    • 35649014840 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 and dysregulated c-Myc cooperatively induce vascular endothelial growth factor and metabolic switches hexokinase 2 and pyruvate dehydrogenase kinase 1
    • Kim J.W., Gao P., Liu Y.C., Semenza G.L., and Dang C.V. Hypoxia-inducible factor 1 and dysregulated c-Myc cooperatively induce vascular endothelial growth factor and metabolic switches hexokinase 2 and pyruvate dehydrogenase kinase 1. Mol Cell Biol 27 (2007) 7381-7393
    • (2007) Mol Cell Biol , vol.27 , pp. 7381-7393
    • Kim, J.W.1    Gao, P.2    Liu, Y.C.3    Semenza, G.L.4    Dang, C.V.5
  • 16
    • 34547225129 scopus 로고    scopus 로고
    • Metabolic targeting of hypoxia and HIF1 in solid tumors can enhance cytotoxic chemotherapy
    • Cairns R.A., Papandreou I., Sutphin P.D., and Denko N.C. Metabolic targeting of hypoxia and HIF1 in solid tumors can enhance cytotoxic chemotherapy. Proc Natl Acad Sci U S A 104 (2007) 9445-9450
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9445-9450
    • Cairns, R.A.1    Papandreou, I.2    Sutphin, P.D.3    Denko, N.C.4
  • 17
    • 43649104579 scopus 로고    scopus 로고
    • Mitochondrial autophagy is an HIF-1-dependent adaptive metabolic response to hypoxia
    • HIF-1 induces BNIP3, which triggers mitochondrial-selective autophagy as a means of reducing ROS generation under hypoxic conditions.
    • Zhang H., Bosch-Marce M., Shimoda L.A., Tan Y.S., Baek J.H., Wesley J.B., Gonzalez F.J., and Semenza G.L. Mitochondrial autophagy is an HIF-1-dependent adaptive metabolic response to hypoxia. J Biol Chem 283 (2008) 10892-10903. HIF-1 induces BNIP3, which triggers mitochondrial-selective autophagy as a means of reducing ROS generation under hypoxic conditions.
    • (2008) J Biol Chem , vol.283 , pp. 10892-10903
    • Zhang, H.1    Bosch-Marce, M.2    Shimoda, L.A.3    Tan, Y.S.4    Baek, J.H.5    Wesley, J.B.6    Gonzalez, F.J.7    Semenza, G.L.8
  • 19
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • The authors show in several cancer cell lines that HIF-1 induces autophagy via expression of both BNIP3 and BNIP3L and, in these cells, knockdown of both proteins was required to block hypoxia-induced autophagy.
    • Bellot G., Garcia-Medina R., Gounon P., Chiche J., Roux D., Pouysségur J., and Mazure N.M. Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol Cell Biol 29 (2009) 2570-2581. The authors show in several cancer cell lines that HIF-1 induces autophagy via expression of both BNIP3 and BNIP3L and, in these cells, knockdown of both proteins was required to block hypoxia-induced autophagy.
    • (2009) Mol Cell Biol , vol.29 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3    Chiche, J.4    Roux, D.5    Pouysségur, J.6    Mazure, N.M.7
  • 20
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda R., Zhang H., Kim J.W., Shimoda L., Dang C.V., and Semenza G.L. HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell 129 (2007) 111-122
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 21
    • 66149179367 scopus 로고    scopus 로고
    • Hypoxia-selective macroautophagy and cell survival signaled by autocrine PDGFR activity
    • Wilkinson S., O'Prey J., Fricker M., and Ryan K.M. Hypoxia-selective macroautophagy and cell survival signaled by autocrine PDGFR activity. Genes Dev 23 (2009) 1283-1288
    • (2009) Genes Dev , vol.23 , pp. 1283-1288
    • Wilkinson, S.1    O'Prey, J.2    Fricker, M.3    Ryan, K.M.4
  • 22
    • 52149101812 scopus 로고    scopus 로고
    • Hypoxia signals autophagy in tumor cells via AMPK activity, independent of HIF-1, BNIP3, and BNIP3L
    • Papandreou I., Lim A.L., Laderoute K., and Denko N.C. Hypoxia signals autophagy in tumor cells via AMPK activity, independent of HIF-1, BNIP3, and BNIP3L. Cell Death Differ 15 (2008) 1572-1581
    • (2008) Cell Death Differ , vol.15 , pp. 1572-1581
    • Papandreou, I.1    Lim, A.L.2    Laderoute, K.3    Denko, N.C.4
  • 23
    • 34247614521 scopus 로고    scopus 로고
    • HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity
    • Zhang H., Gao P., Fukuda R., Kumar G., Krishnamachary B., Zeller K.I., Dang C.V., and Semenza G.L. HIF-1 inhibits mitochondrial biogenesis and cellular respiration in VHL-deficient renal cell carcinoma by repression of C-MYC activity. Cancer Cell 11 (2007) 407-420
    • (2007) Cancer Cell , vol.11 , pp. 407-420
    • Zhang, H.1    Gao, P.2    Fukuda, R.3    Kumar, G.4    Krishnamachary, B.5    Zeller, K.I.6    Dang, C.V.7    Semenza, G.L.8
  • 24
  • 25
    • 67650480092 scopus 로고    scopus 로고
    • mTOR and HIF-1α-mediated tumor metabolism in an LKB1 mouse model of Peutz-Jeghers syndrome
    • The authors connect LKB1 loss of function with mTOR and HIF-1 gain of function, glucose uptake and gastrointestinal neoplasia.
    • Shackelford D.B., Vasquez D.S., Corbeil J., Wu S., Leblanc M., Wu C.L., Vera D.R., and Shaw R.J. mTOR and HIF-1α-mediated tumor metabolism in an LKB1 mouse model of Peutz-Jeghers syndrome. Proc Natl Acad Sci U S A 106 (2009) 11137-11142. The authors connect LKB1 loss of function with mTOR and HIF-1 gain of function, glucose uptake and gastrointestinal neoplasia.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 11137-11142
    • Shackelford, D.B.1    Vasquez, D.S.2    Corbeil, J.3    Wu, S.4    Leblanc, M.5    Wu, C.L.6    Vera, D.R.7    Shaw, R.J.8
  • 27
    • 0034654174 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor 1α expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: implications for tumor angiogenesis and therapeutics
    • Zhong H., Chiles K., Feldser D., Laughner E., Hanrahan C., Georgescu M.M., Simons J.W., and Semenza G.L. Modulation of hypoxia-inducible factor 1α expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: implications for tumor angiogenesis and therapeutics. Cancer Res 60 (2000) 1541-1545
    • (2000) Cancer Res , vol.60 , pp. 1541-1545
    • Zhong, H.1    Chiles, K.2    Feldser, D.3    Laughner, E.4    Hanrahan, C.5    Georgescu, M.M.6    Simons, J.W.7    Semenza, G.L.8
  • 29
    • 3142587052 scopus 로고    scopus 로고
    • Dysregulation of HIF and VEGF is a unifying feature of the familial hamartoma syndromes
    • Brugarolas J., and Kaelin Jr. W.G. Dysregulation of HIF and VEGF is a unifying feature of the familial hamartoma syndromes. Cancer Cell 6 (2004) 7-10
    • (2004) Cancer Cell , vol.6 , pp. 7-10
    • Brugarolas, J.1    Kaelin Jr., W.G.2
  • 30
    • 0035012605 scopus 로고    scopus 로고
    • HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1α (HIF-1α) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression
    • Laughner E., Taghavi P., Chiles K., Mahon P.C., and Semenza G.L. HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1α (HIF-1α) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression. Mol Cell Biol 21 (2001) 3995-4004
    • (2001) Mol Cell Biol , vol.21 , pp. 3995-4004
    • Laughner, E.1    Taghavi, P.2    Chiles, K.3    Mahon, P.C.4    Semenza, G.L.5
  • 33
    • 23644448721 scopus 로고    scopus 로고
    • HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability
    • Isaacs J.S., Jung Y.J., Mole D.R., Lee S., Torres-Cabala C., Chung Y.L., Merino M., Trepel J., Zbar B., Toro J., et al. HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability. Cancer Cell 8 (2005) 143-153
    • (2005) Cancer Cell , vol.8 , pp. 143-153
    • Isaacs, J.S.1    Jung, Y.J.2    Mole, D.R.3    Lee, S.4    Torres-Cabala, C.5    Chung, Y.L.6    Merino, M.7    Trepel, J.8    Zbar, B.9    Toro, J.10
  • 34
    • 33947520506 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF
    • Koivunen P., Hirsilä M., Remes A.M., Hassinen I.E., Kivirikko K.I., and Myllyharju J. Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF. J Biol Chem 282 (2007) 4524-4532
    • (2007) J Biol Chem , vol.282 , pp. 4524-4532
    • Koivunen, P.1    Hirsilä, M.2    Remes, A.M.3    Hassinen, I.E.4    Kivirikko, K.I.5    Myllyharju, J.6
  • 35
    • 34047255064 scopus 로고    scopus 로고
    • Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates
    • Hewitson K.S., Liénard B.M., McDonough M.A., Clifton I.J., Butler D., Soares A.S., Oldham N.J., McNeill L.A., and Schofield C.J. Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. J Biol Chem 282 (2007) 3293-3301
    • (2007) J Biol Chem , vol.282 , pp. 3293-3301
    • Hewitson, K.S.1    Liénard, B.M.2    McDonough, M.A.3    Clifton, I.J.4    Butler, D.5    Soares, A.S.6    Oldham, N.J.7    McNeill, L.A.8    Schofield, C.J.9
  • 36
    • 64849098267 scopus 로고    scopus 로고
    • Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1α
    • Missense mutations in the IDH1 gene occur in secondary glioblastoma and impair the enzyme's affinity for its substrate. Forced expression of mutant IDH1 in cultured cells reduces formation of the enzyme product, α-ketoglutarate, and thereby increases HIF-1α levels.
    • Zhao S., Lin Y., Xu W., Jiang W., Zha Z., Wang P., Yu W., Li Z., Gong L., Peng Y., et al. Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1α. Science 324 (2009) 261-265. Missense mutations in the IDH1 gene occur in secondary glioblastoma and impair the enzyme's affinity for its substrate. Forced expression of mutant IDH1 in cultured cells reduces formation of the enzyme product, α-ketoglutarate, and thereby increases HIF-1α levels.
    • (2009) Science , vol.324 , pp. 261-265
    • Zhao, S.1    Lin, Y.2    Xu, W.3    Jiang, W.4    Zha, Z.5    Wang, P.6    Yu, W.7    Li, Z.8    Gong, L.9    Peng, Y.10
  • 37
    • 59449106196 scopus 로고    scopus 로고
    • Mitochondrial mutations contribute to HIF-1α accumulation via increased reactive oxygen species and up-regulated pyruvate dehydrogenase kinase 2 in head and neck squamous cell carcinoma
    • Sun W., Zhou S., Chang S.S., McFate T., Verma A., and Califano J.A. Mitochondrial mutations contribute to HIF-1α accumulation via increased reactive oxygen species and up-regulated pyruvate dehydrogenase kinase 2 in head and neck squamous cell carcinoma. Clin Cancer Res 15 (2009) 476-484
    • (2009) Clin Cancer Res , vol.15 , pp. 476-484
    • Sun, W.1    Zhou, S.2    Chang, S.S.3    McFate, T.4    Verma, A.5    Califano, J.A.6
  • 39
    • 53049087909 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells
    • The authors provide evidence of a feed-forward mechanism in which increased HIF-1 activity induces expression of PDK1, which alters levels of glycolytic metabolites, which in turn further increase HIF-1 activity.
    • McFate T., Mohyeldin A., Lu H., Thakar J., Henriques J., Halim N.D., Wu H., Schell M.J., Tsang T.M., Teahan O., et al. Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. J Biol Chem 283 (2008) 22700-22708. The authors provide evidence of a feed-forward mechanism in which increased HIF-1 activity induces expression of PDK1, which alters levels of glycolytic metabolites, which in turn further increase HIF-1 activity.
    • (2008) J Biol Chem , vol.283 , pp. 22700-22708
    • McFate, T.1    Mohyeldin, A.2    Lu, H.3    Thakar, J.4    Henriques, J.5    Halim, N.D.6    Wu, H.7    Schell, M.J.8    Tsang, T.M.9    Teahan, O.10
  • 40
    • 60949102817 scopus 로고    scopus 로고
    • Hypoxia inducible factor-2α: a critical mediator of aggressive tumor phenotypes
    • Qing G., and Simon M.C. Hypoxia inducible factor-2α: a critical mediator of aggressive tumor phenotypes. Curr Opin Genet Dev 19 (2009) 60-66
    • (2009) Curr Opin Genet Dev , vol.19 , pp. 60-66
    • Qing, G.1    Simon, M.C.2
  • 42
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2α signaling by the stress-responsive deacetylase sirtuin 1
    • The authors show that SIRT1 is a positive regulator of HIF-2α. It appears that SIRT1 can have oncogenic or tumor suppressor effects, depending upon the particular context [46], as is also true for HIF-2α [47].
    • Dioum E.M., Chen R., Alexander M.S., Zhang Q., Hogg R.T., Gerard R.D., and Garcia J.A. Regulation of hypoxia-inducible factor 2α signaling by the stress-responsive deacetylase sirtuin 1. Science 324 (2009) 1289-1293. The authors show that SIRT1 is a positive regulator of HIF-2α. It appears that SIRT1 can have oncogenic or tumor suppressor effects, depending upon the particular context [46], as is also true for HIF-2α [47].
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3    Zhang, Q.4    Hogg, R.T.5    Gerard, R.D.6    Garcia, J.A.7
  • 43
    • 40349108704 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 promotes tumor cell survival by coactivating hypoxia-inducible factor-1-dependent gene expression
    • Elser M., Borsig L., Hassa P.O., Erener S., Messner S., Valovka T., Keller S., Gassmann M., and Hottiger M.O. Poly(ADP-ribose) polymerase 1 promotes tumor cell survival by coactivating hypoxia-inducible factor-1-dependent gene expression. Mol Cancer Res 6 (2008) 282-290
    • (2008) Mol Cancer Res , vol.6 , pp. 282-290
    • Elser, M.1    Borsig, L.2    Hassa, P.O.3    Erener, S.4    Messner, S.5    Valovka, T.6    Keller, S.7    Gassmann, M.8    Hottiger, M.O.9
  • 44
    • 31544473721 scopus 로고    scopus 로고
    • Nitric oxide is a factor in the stabilization of hypoxia-inducible factor-1α in cancer: role of free radical formation
    • Quintero M., Brennan P.A., Thomas G.J., and Moncada S. Nitric oxide is a factor in the stabilization of hypoxia-inducible factor-1α in cancer: role of free radical formation. Cancer Res 66 (2006) 770-774
    • (2006) Cancer Res , vol.66 , pp. 770-774
    • Quintero, M.1    Brennan, P.A.2    Thomas, G.J.3    Moncada, S.4
  • 45
    • 66449130218 scopus 로고    scopus 로고
    • Endothelial NOS, estrogen receptor β, and HIFs cooperate in the activation of a prognostic transcriptional pattern in aggressive human prostate cancer
    • The authors demonstrate that overexpressed and nuclear-localized endothelial NOS promotes the transcriptional activity of ER-β, HIF-1α, and HIF-2α, which cooperate to activate transcription of genes associated with poor prognosis in prostate cancer. The study is an elegant blend of clinical and molecular approaches. The immunohistochemical and gene expression analyses described in this study could be used to identify prostate cancer patients who might be particularly likely to benefit from treatment with NOS and/or HIF-1 inhibitors.
    • Nanni S., Benvenuti V., Grasselli A., Priolo C., Aiello A., Mattiussi S., Colussi C., Lirangi V., Illi B., D'Eletto M., et al. Endothelial NOS, estrogen receptor β, and HIFs cooperate in the activation of a prognostic transcriptional pattern in aggressive human prostate cancer. J Clin Invest 119 (2009) 1093-1108. The authors demonstrate that overexpressed and nuclear-localized endothelial NOS promotes the transcriptional activity of ER-β, HIF-1α, and HIF-2α, which cooperate to activate transcription of genes associated with poor prognosis in prostate cancer. The study is an elegant blend of clinical and molecular approaches. The immunohistochemical and gene expression analyses described in this study could be used to identify prostate cancer patients who might be particularly likely to benefit from treatment with NOS and/or HIF-1 inhibitors.
    • (2009) J Clin Invest , vol.119 , pp. 1093-1108
    • Nanni, S.1    Benvenuti, V.2    Grasselli, A.3    Priolo, C.4    Aiello, A.5    Mattiussi, S.6    Colussi, C.7    Lirangi, V.8    Illi, B.9    D'Eletto, M.10
  • 46
    • 68949113934 scopus 로고    scopus 로고
    • SirT1-null mice develop tumors at normal rates but are poorly protected by resveratrol
    • Boily G., He X.H., Pearce B., Jardine K., and McBurney M.W. SirT1-null mice develop tumors at normal rates but are poorly protected by resveratrol. Oncogene 28 (2009) 2882-2893
    • (2009) Oncogene , vol.28 , pp. 2882-2893
    • Boily, G.1    He, X.H.2    Pearce, B.3    Jardine, K.4    McBurney, M.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.