메뉴 건너뛰기




Volumn , Issue , 2012, Pages

TCA cycle defects and cancer: When metabolism tunes redox state

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; FUMARATE HYDRATASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; ISOCITRATE DEHYDROGENASE; SUCCINATE DEHYDROGENASE;

EID: 84864950181     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2012/161837     Document Type: Review
Times cited : (130)

References (80)
  • 1
    • 44449147036 scopus 로고    scopus 로고
    • Tumor Cell Metabolism: Cancer's Achilles' Heel
    • DOI 10.1016/j.ccr.2008.05.005, PII S1535610808001608
    • Kroemer G., Pouyssegur J., Tumor cell metabolism: Cancer's Achilles' heel Cancer Cell 2008 13 6 472 482 (Pubitemid 351766797)
    • (2008) Cancer Cell , vol.13 , Issue.6 , pp. 472-482
    • Kroemer, G.1    Pouyssegur, J.2
  • 2
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O., On the origin of cancer cells Science 1956 123 3191 309 314
    • (1956) Science , vol.123 , Issue.3191 , pp. 309-314
    • Warburg, O.1
  • 4
    • 83755178091 scopus 로고
    • Hypoxia promotes isocytrate dehydrogenase-dependent carboxylation of -ketoglutarate to citrate to support cell growth and viability
    • 19616
    • Wise D. R., Ward P. S., Shay J. E., Hypoxia promotes isocytrate dehydrogenase-dependent carboxylation of -ketoglutarate to citrate to support cell growth and viability Proceedings of the National Academy of Sciences USA 1961 108 49 19611 19616
    • (1961) Proceedings of the National Academy of Sciences USA , vol.108 , Issue.49 , pp. 19611
    • Wise, D.R.1    Ward, P.S.2    Shay, J.E.3
  • 5
    • 84856014884 scopus 로고    scopus 로고
    • Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia
    • Metallo C. M., Gameiro P. A., Bell E. L., Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia Nature 2011 481 7381 380 384
    • (2011) Nature , vol.481 , Issue.7381 , pp. 380-384
    • Metallo, C.M.1    Gameiro, P.A.2    Bell, E.L.3
  • 6
    • 84855987831 scopus 로고    scopus 로고
    • Reductive carboxylation supports growth in tumour cells with defective mitochondria
    • Mullen A. R., Wheaton W. W., Jin E. S., Reductive carboxylation supports growth in tumour cells with defective mitochondria Nature 2011 481 7381 385 388
    • (2011) Nature , vol.481 , Issue.7381 , pp. 385-388
    • Mullen, A.R.1    Wheaton, W.W.2    Jin, E.S.3
  • 10
    • 0033767445 scopus 로고    scopus 로고
    • Mutations in SDHC cause autosomal dominant paraganglioma, type 3
    • Niemann S., Mller U., Mutations in SDHC cause autosomal dominant paraganglioma, type 3 Nature Genetics 2000 26 3 268 270
    • (2000) Nature Genetics , vol.26 , Issue.3 , pp. 268-270
    • Niemann, S.1    Mller, U.2
  • 16
    • 28544446058 scopus 로고    scopus 로고
    • Mitochondrial tumour suppressors: A genetic and biochemical update
    • DOI 10.1038/nrc1737
    • Gottlieb E., Tomlinson I. P. M., Mitochondrial tumour suppressors: a genetic and biochemical update Nature Reviews Cancer 2005 5 11 857 866 (Pubitemid 41746030)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.11 , pp. 857-866
    • Gottlieb, E.1    Tomlinson, I.P.M.2
  • 17
    • 0022534603 scopus 로고
    • Fumarase deficiency: A new cause of mitochondrial encephalomyopathy
    • Zinn A. B., Kerr D. S., Hoppel C. L., Fumarase deficiency: a new cause of mitochondrial encephalomyopathy The New England Journal of Medicine 1986 315 8 469 475 (Pubitemid 16034147)
    • (1986) New England Journal of Medicine , vol.315 , Issue.8 , pp. 469-475
    • Zinn, A.B.1    Kerr, D.S.2    Hoppel, C.L.3
  • 22
    • 33746930794 scopus 로고    scopus 로고
    • Succinate dehydrogenase and fumarate hydratase: Linking mitochondrial dysfunction and cancer
    • DOI 10.1038/sj.onc.1209594, PII 1209594
    • King A., Selak M. A., Gottlieb E., Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer Oncogene 2006 25 34 4675 4682 (Pubitemid 44187617)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4675-4682
    • King, A.1    Selak, M.A.2    Gottlieb, E.3
  • 23
    • 77956265489 scopus 로고    scopus 로고
    • IDH mutations in glioma and acute myeloid leukemia
    • Dang L., Jin S., Su S. M., IDH mutations in glioma and acute myeloid leukemia Trends in Molecular Medicine 2010 16 9 392 397
    • (2010) Trends in Molecular Medicine , vol.16 , Issue.9 , pp. 392-397
    • Dang, L.1    Jin, S.2    Su, S.M.3
  • 26
    • 84857575341 scopus 로고    scopus 로고
    • IDH2 mutations are frequent in angioimmunoblastic T-cell lymphoma
    • Cairns R. A., Iqbal J., Lemonnier F., IDH2 mutations are frequent in angioimmunoblastic T-cell lymphoma Blood 2012 119 8 1901 1903
    • (2012) Blood , vol.119 , Issue.8 , pp. 1901-1903
    • Cairns, R.A.1    Iqbal, J.2    Lemonnier, F.3
  • 28
    • 77955907891 scopus 로고    scopus 로고
    • IDH1 and IDH2 mutations are frequent genetic alterations in acute myeloid leukemia and confer adverse prognosis in cytogenetically normal acute myeloid leukemia with NPM1 mutation without FLT3 internal tandem duplication
    • Paschka P., Schlenk R. F., Gaidzik V. I., Habdank M., Krnke J., Bullinger L., Spth D., Kayser S., Zucknick M., Gtze K., Horst H. A., Germing U., Dhner H., Dhner K., IDH1 and IDH2 mutations are frequent genetic alterations in acute myeloid leukemia and confer adverse prognosis in cytogenetically normal acute myeloid leukemia with NPM1 mutation without FLT3 internal tandem duplication Journal of Clinical Oncology 2010 28 22 3636 3643
    • (2010) Journal of Clinical Oncology , vol.28 , Issue.22 , pp. 3636-3643
    • Paschka, P.1    Schlenk, R.F.2    Gaidzik, V.I.3    Habdank, M.4    Krnke, J.5    Bullinger, L.6    Spth, D.7    Kayser, S.8    Zucknick, M.9    Gtze, K.10    Horst, H.A.11    Germing, U.12    Dhner, H.13    Dhner, K.14
  • 30
    • 78649990315 scopus 로고    scopus 로고
    • Cancer-associated IDH mutations: Biomarker and therapeutic opportunities
    • Yen K. E., Bittinger M. A., Su S. M., Fantin V. R., Cancer-associated IDH mutations: biomarker and therapeutic opportunities Oncogene 2010 29 49 6409 6417
    • (2010) Oncogene , vol.29 , Issue.49 , pp. 6409-6417
    • Yen, K.E.1    Bittinger, M.A.2    Su, S.M.3    Fantin, V.R.4
  • 33
    • 0035213138 scopus 로고    scopus 로고
    • The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway
    • DOI 10.1086/324413
    • Gimenez-Roqueplo A. P., Favier J., Rustin P., Mourad J. J., Plouin P. F., Corvol P., Rtig A., Jeunemaitre X., The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway American Journal of Human Genetics 2001 69 6 1186 1197 (Pubitemid 33124200)
    • (2001) American Journal of Human Genetics , vol.69 , Issue.6 , pp. 1186-1197
    • Gimenez-Roqueplo, A.-P.1    Favier, J.2    Rustin, P.3    Mourad, J.-J.4    Plouin, P.-F.5    Corvol, P.6    Rotig, A.7    Jeunemaitre, X.8
  • 37
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one?
    • Ozer A., Bruick R. K., Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nature Chemical Biology 2007 3 3 144 153
    • (2007) Nature Chemical Biology , vol.3 , Issue.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 39
    • 80054767730 scopus 로고    scopus 로고
    • Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: Roles for fumarate in KEAP1 succination and Nrf2 signaling
    • Adam J., Hatipoglu E., O'Flaherty L., Renal cyst formation in Fh1-deficient mice is independent of the Hif/Phd pathway: roles for fumarate in KEAP1 succination and Nrf2 signaling Cancer Cell 2011 20 4 524 537
    • (2011) Cancer Cell , vol.20 , Issue.4 , pp. 524-537
    • Adam, J.1    Hatipoglu, E.2    O'Flaherty, L.3
  • 40
    • 84862776918 scopus 로고    scopus 로고
    • Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation
    • Koivunen P., Lee S., Duncan C. G., Kaelin C. G. Jr., Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation Nature 2012 483 484 488
    • (2012) Nature , vol.483 , pp. 484-488
    • Koivunen, P.1    Lee, S.2    Duncan, C.G.3    Kaelin Jr., C.G.4
  • 41
    • 23644436667 scopus 로고    scopus 로고
    • Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: Developmental culling and cancer
    • DOI 10.1016/j.ccr.2005.06.015, PII S1535610805002242
    • Lee S., Nakamura E., Yang H., Wei W., Linggi M. S., Sajan M. P., Farese R. V., Freeman R. S., Carter B. D., Kaelin W. G., Schlisio S., Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer Cancer Cell 2005 8 2 155 167 (Pubitemid 41132744)
    • (2005) Cancer Cell , vol.8 , Issue.2 , pp. 155-167
    • Lee, S.1    Nakamura, E.2    Yang, H.3    Wei, W.4    Linggi, M.S.5    Sajan, M.P.6    Farese, R.V.7    Freeman, R.S.8    Carter, B.D.9    Kaelin Jr., W.G.10    Schlisio, S.11
  • 43
    • 77953995002 scopus 로고    scopus 로고
    • Covalent histone modifications-miswritten, misinterpreted and mis-erased in human cancers
    • Chi P., Allis C. D., Wang G. G., Covalent histone modifications- miswritten, misinterpreted and mis-erased in human cancers Nature Reviews Cancer 2010 10 7 457 469
    • (2010) Nature Reviews Cancer , vol.10 , Issue.7 , pp. 457-469
    • Chi, P.1    Allis, C.D.2    Wang, G.G.3
  • 44
    • 79959539769 scopus 로고    scopus 로고
    • Epigenetic regulation in cancer development
    • Caffarelli E., Filetici P., Epigenetic regulation in cancer development Frontiers in Bioscience 2011 1 17 2682 2694
    • (2011) Frontiers in Bioscience , vol.1 , Issue.17 , pp. 2682-2694
    • Caffarelli, E.1    Filetici, P.2
  • 45
    • 78649664485 scopus 로고    scopus 로고
    • Structural insights into histone lysine demethylation
    • Hou H., Yu H., Structural insights into histone lysine demethylation Current Opinion in Structural Biology 2010 20 6 739 748
    • (2010) Current Opinion in Structural Biology , vol.20 , Issue.6 , pp. 739-748
    • Hou, H.1    Yu, H.2
  • 46
    • 70450239624 scopus 로고    scopus 로고
    • Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells
    • Cervera A. M., Bayley J. P., Devilee P., McCreath K. J., Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells Molecular Cancer 2009 8, article 89
    • (2009) Molecular Cancer , vol.889
    • Cervera, A.M.1    Bayley, J.P.2    Devilee, P.3    McCreath, K.J.4
  • 47
    • 36249005491 scopus 로고    scopus 로고
    • Succinate inhibition of -ketoglutarate-dependent enzymes in a yeast model of paraganglioma
    • DOI 10.1093/hmg/ddm275
    • Smith E. H., Janknecht R., Maher J. L. III, Succinate inhibition of -ketoglutarate-dependent enzymes in a yeast model of paraganglioma Human Molecular Genetics 2007 16 24 3136 3148 (Pubitemid 350131331)
    • (2007) Human Molecular Genetics , vol.16 , Issue.24 , pp. 3136-3148
    • Smith, E.H.1    Janknecht, R.2    Maher III, J.L.3
  • 50
    • 79961172608 scopus 로고    scopus 로고
    • Histone onco-modifications
    • Fllgrabe J., Kavanagh E., Joseph B., Histone onco-modifications Oncogene 2011 30 31 3391 3403
    • (2011) Oncogene , vol.30 , Issue.31 , pp. 3391-3403
    • Fllgrabe, J.1    Kavanagh, E.2    Joseph, B.3
  • 51
    • 84857443720 scopus 로고    scopus 로고
    • Cellular epigenetic stability and cancer
    • Sarkies P., Sale J. E., Cellular epigenetic stability and cancer Trends in Genetics 2012 28 3 118 127
    • (2012) Trends in Genetics , vol.28 , Issue.3 , pp. 118-127
    • Sarkies, P.1    Sale, J.E.2
  • 52
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski T. P., Nathan C. F., Production of large amounts of hydrogen peroxide by human tumor cells Cancer Research 1991 51 3 794 798
    • (1991) Cancer Research , vol.51 , Issue.3 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 53
    • 0028900690 scopus 로고
    • Persistent oxidative stress in cancer
    • Toyokuni S., Persistent oxidative stress in cancer FEBS Letters 1995 358 1 1 3
    • (1995) FEBS Letters , vol.358 , Issue.1 , pp. 1-3
    • Toyokuni, S.1
  • 54
    • 33745489431 scopus 로고    scopus 로고
    • Oxidative and nitrative DNA damage in animals and patients with inflammatory diseases in relation to inflammation-related carcinogenesis
    • Kawanishi S., Hiraku Y., Pinlaor S., Ma N., Oxidative and nitrative DNA damage in animals and patients with inflammatory diseases in relation to inflammation-related carcinogenesis Biological Chemistry 2006 387 4 365 372
    • (2006) Biological Chemistry , vol.387 , Issue.4 , pp. 365-372
    • Kawanishi, S.1    Hiraku, Y.2    Pinlaor, S.3    Ma, N.4
  • 55
    • 0032514466 scopus 로고    scopus 로고
    • A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes
    • DOI 10.1038/29331
    • Ishii N., Fujii M., Hartman P. S., Tsuda M., Yasuda K., Senoo-Matsuda N., Yanase S., Ayusawa D., Suzuki K., A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes Nature 1998 394 6694 694 697 (Pubitemid 28389798)
    • (1998) Nature , vol.394 , Issue.6694 , pp. 694-697
    • Ishii, N.1    Fujii, M.2    Hartman, P.S.3    Tsuda, M.4    Yasuda, K.5    Senoo-Matsuda, N.6    Yanase, S.7    Ayusawa, D.8    Suzuki, K.9
  • 56
    • 0035834789 scopus 로고    scopus 로고
    • A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in caenorhabditis elegans
    • Senoo-Matsuda N., Yasuda K., Tsuda M., Ohkubo T., Yoshimura S., Nakazawa H., Hartman P. S., Ishii N., A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in caenorhabditis elegans The Journal of Biological Chemistry 2001 276 45 41553 41558
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.45 , pp. 41553-41558
    • Senoo-Matsuda, N.1    Yasuda, K.2    Tsuda, M.3    Ohkubo, T.4    Yoshimura, S.5    Nakazawa, H.6    Hartman, P.S.7    Ishii, N.8
  • 57
    • 11244279161 scopus 로고    scopus 로고
    • A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis
    • Ishii T., Yasuda K., Akatsuka A., Hino O., Hartman P. S., Ishii N., A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis Cancer Research 2005 65 1 203 209 (Pubitemid 40070811)
    • (2005) Cancer Research , vol.65 , Issue.1 , pp. 203-209
    • Ishii, T.1    Yasuda, K.2    Akatsuka, A.3    Hino, O.4    Hartman, P.S.5    Ishii, N.6
  • 58
    • 37849022071 scopus 로고    scopus 로고
    • Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis
    • Guzy R. D., Sharma B., Bell E., Chandel N. S., Schumacker P. T., Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis Molecular and Cellular Biology 2008 28 2 718 731
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.2 , pp. 718-731
    • Guzy, R.D.1    Sharma, B.2    Bell, E.3    Chandel, N.S.4    Schumacker, P.T.5
  • 60
  • 61
    • 27944442839 scopus 로고    scopus 로고
    • Disulfide relays and phosphorylative cascades: Partners in redox-mediated signaling pathways
    • DOI 10.1038/sj.cdd.4401754, PII 4401754
    • Filomeni G., Rotilio G., Ciriolo M. R., Disulfide relays and phosphorylative cascades: partners in redox-mediated signaling pathways Cell Death and Differentiation 2005 12 12 1555 1563 (Pubitemid 41679161)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.12 , pp. 1555-1563
    • Filomeni, G.1    Rotilio, G.2    Ciriolo, M.R.3
  • 67
  • 70
    • 80054772589 scopus 로고    scopus 로고
    • An antioxidant response phenotype shared between hereditary and sporadic type 2 papillary renal cell carcinoma
    • Ooi A., Wong J. C., Petillo D., An antioxidant response phenotype shared between hereditary and sporadic type 2 papillary renal cell carcinoma Cancer Cell 2011 20 4 511 523
    • (2011) Cancer Cell , vol.20 , Issue.4 , pp. 511-523
    • Ooi, A.1    Wong, J.C.2    Petillo, D.3
  • 71
    • 77958115724 scopus 로고    scopus 로고
    • Regulation of the Nrf2-keap1 antioxidant response by the ubiquitin proteasome system: An insight into cullin-ring ubiquitin ligases
    • Villeneuve N. F., Lau A., Zhang D. D., Regulation of the Nrf2-keap1 antioxidant response by the ubiquitin proteasome system: an insight into cullin-ring ubiquitin ligases Antioxidants and Redox Signaling 2010 13 11 1699 1712
    • (2010) Antioxidants and Redox Signaling , vol.13 , Issue.11 , pp. 1699-1712
    • Villeneuve, N.F.1    Lau, A.2    Zhang, D.D.3
  • 72
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer
    • Hayes J. D., McMahon M., NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer Trends in Biochemical Sciences 2009 34 4 176 188
    • (2009) Trends in Biochemical Sciences , vol.34 , Issue.4 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 74
    • 80052580351 scopus 로고    scopus 로고
    • Haem oxygenase is synthetically lethal with the tumour suppressor fumarate hydratase
    • Frezza C., Zheng L., Folger O., Haem oxygenase is synthetically lethal with the tumour suppressor fumarate hydratase Nature 2011 477 7363 225 228
    • (2011) Nature , vol.477 , Issue.7363 , pp. 225-228
    • Frezza, C.1    Zheng, L.2    Folger, O.3
  • 77
    • 45549090890 scopus 로고    scopus 로고
    • Genetic basis for kidney cancer: Opportunity for disease-specific approaches to therapy
    • DOI 10.1517/14712598.8.6.779
    • Pfaffenroth E. C., Linehan W. M., Genetic basis for kidney cancer: opportunity for disease-specific approaches to therapy Expert Opinion on Biological Therapy 2008 8 6 779 790 (Pubitemid 351860207)
    • (2008) Expert Opinion on Biological Therapy , vol.8 , Issue.6 , pp. 779-790
    • Pfaffenroth, E.C.1    Linehan, W.M.2
  • 79
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • DOI 10.1016/S0891-5849(01)00480-4, PII S0891584901004804
    • Schafer F. Q., Buettner G. R., Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radical Biology and Medicine 2001 30 11 1191 1212 (Pubitemid 32463931)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.11 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.