메뉴 건너뛰기




Volumn 35, Issue 8, 2003, Pages 634-635

The TCA cycle and tumorigenesis: The examples of fumarate hydratase and succinate dehydrogenase

Author keywords

Apoptosis; Fibroid; Fumarate hydratase; Hypoxia; Krebs TCA cycle; Leiomyoma; Mitochondria; Oxidative stress; Paraganglioma; Phaeochromocytoma; Renal cell carcinoma; Succinate dehydrogenase; Tumorigenesis; Tumour suppressor

Indexed keywords

ADENOSINE TRIPHOSPHATE; FUMARATE HYDRATASE; SUCCINATE DEHYDROGENASE;

EID: 0348107409     PISSN: 07853890     EISSN: None     Source Type: Journal    
DOI: 10.1080/07853890310018458     Document Type: Review
Times cited : (123)

References (48)
  • 1
    • 0031867909 scopus 로고    scopus 로고
    • Familial multiple symmetric lipomatosis associated with the A8344G mutation of mitochondrial DNA
    • Gamez J, Playan A, Andreu AL, Bruno C, Navarro C, Cervera C, et al. Familial multiple symmetric lipomatosis associated with the A8344G mutation of mitochondrial DNA. Neurology 1998;51:258-60.
    • (1998) Neurology , vol.51 , pp. 258-260
    • Gamez, J.1    Playan, A.2    Andreu, A.L.3    Bruno, C.4    Navarro, C.5    Cervera, C.6
  • 4
    • 0025261176 scopus 로고
    • Fumarase deficiency is an autosomal recessive encephalopathy affecting both the mitochondrial and the cytosolic enzymes
    • Gellera C, Uziel G, Rimoldi M, Zeviani M, Laverda A, Carrara F, et al. Fumarase deficiency is an autosomal recessive encephalopathy affecting both the mitochondrial and the cytosolic enzymes. Neurology 1990;40:495-9.
    • (1990) Neurology , vol.40 , pp. 495-499
    • Gellera, C.1    Uziel, G.2    Rimoldi, M.3    Zeviani, M.4    Laverda, A.5    Carrara, F.6
  • 5
    • 0028246154 scopus 로고
    • Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency
    • Jun
    • Bourgeron T, Chretien D, Poggi-Bach J, Doonan S, Rabier D, Letouze P, et al. Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiency. J Clin Invest 1994 Jun;93(6)2514-8.
    • (1994) J Clin Invest , vol.93 , Issue.6 , pp. 2514-2518
    • Bourgeron, T.1    Chretien, D.2    Poggi-Bach, J.3    Doonan, S.4    Rabier, D.5    Letouze, P.6
  • 6
    • 0035007528 scopus 로고    scopus 로고
    • Localization of a gene (MCUL1) for multiple cutaneous leiomyomata and uterine fibroids to chromosome 1q42.3-q43
    • Alam NA, Bevan S, Churchman M, Barclay E, Barker K, Jaeger EE, et al. Localization of a gene (MCUL1) for multiple cutaneous leiomyomata and uterine fibroids to chromosome 1q42.3-q43. Am J Hum Genet 2001;68:1264-9.
    • (2001) Am J Hum Genet , vol.68 , pp. 1264-1269
    • Alam, N.A.1    Bevan, S.2    Churchman, M.3    Barclay, E.4    Barker, K.5    Jaeger, E.E.6
  • 7
    • 18544365990 scopus 로고    scopus 로고
    • Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer
    • Tomlinson IP, Alam NA, Rowan AJ, Barclay E, Jaeger EE, Kelsell D, et al. Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer. Nat Genet 2002;30:406-10.
    • (2002) Nat Genet , vol.30 , pp. 406-410
    • Tomlinson, I.P.1    Alam, N.A.2    Rowan, A.J.3    Barclay, E.4    Jaeger, E.E.5    Kelsell, D.6
  • 8
    • 0034849758 scopus 로고    scopus 로고
    • Familial cutaneous leiomyomatosis is a two-hit condition associated with renal cell cancer of characteristic histopathology
    • Kiuru M, Launonen V, Hietala M, Aittomaki K, Vierimaa O, Salovaara R, et al. Familial cutaneous leiomyomatosis is a two-hit condition associated with renal cell cancer of characteristic histopathology. Am J Pathol 2001;159:825-9.
    • (2001) Am J Pathol , vol.159 , pp. 825-829
    • Kiuru, M.1    Launonen, V.2    Hietala, M.3    Aittomaki, K.4    Vierimaa, O.5    Salovaara, R.6
  • 10
    • 0037102441 scopus 로고    scopus 로고
    • Few FH mutations in sporadic counterparts of tumor types observed in hereditary leiomyomatosis and renal cell cancer families
    • Kiuru M, Lehtonen R, Arola J, Salovaara R, Jarvinen H, Aittomaki K, et al. Few FH mutations in sporadic counterparts of tumor types observed in hereditary leiomyomatosis and renal cell cancer families. Cancer Res 2002;62:4554-7.
    • (2002) Cancer Res , vol.62 , pp. 4554-4557
    • Kiuru, M.1    Lehtonen, R.2    Arola, J.3    Salovaara, R.4    Jarvinen, H.5    Aittomaki, K.6
  • 11
    • 18544365098 scopus 로고    scopus 로고
    • Low frequency of somatic mutations in the FH/ multiple cutaneous leiomyomatosis gene in sporadic leiomyosarcomas and uterine leiomyomas
    • Barker KT, Bevan S, Wang R, Lu YJ, Flanagan AM, Bridge JA, et al. Low frequency of somatic mutations in the FH/ multiple cutaneous leiomyomatosis gene in sporadic leiomyosarcomas and uterine leiomyomas. Br J Cancer 2002;87:446-8.
    • (2002) Br J Cancer , vol.87 , pp. 446-448
    • Barker, K.T.1    Bevan, S.2    Wang, R.3    Lu, Y.J.4    Flanagan, A.M.5    Bridge, J.A.6
  • 12
    • 12444259659 scopus 로고    scopus 로고
    • Genetic and functional analyses of FH mutations in multiple cutaneous and uterine leiomyomatosis, hereditary leiomyomatosis and renal cancer, and fumarate hydratase deficiency
    • Alam NA, Rowan AJ, Wortham NC, Pollard PJ, Mitchell M, Tyrer JP, et al. Genetic and functional analyses of FH mutations in multiple cutaneous and uterine leiomyomatosis, hereditary leiomyomatosis and renal cancer, and fumarate hydratase deficiency. Hum Mol Genet 2003;12:1241-52.
    • (2003) Hum Mol Genet , vol.12 , pp. 1241-1252
    • Alam, N.A.1    Rowan, A.J.2    Wortham, N.C.3    Pollard, P.J.4    Mitchell, M.5    Tyrer, J.P.6
  • 13
    • 0029159804 scopus 로고
    • Mutation of a nuclear succinace dehydrogenase gene results in mitochondrial respiratory chain deficiency
    • Bourgeron T, Rustin P, Chretien D, Birch-Machin M, Bourgeois M, Viegas-Pequignot E, et al. Mutation of a nuclear succinace dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nat Genet 1995;11:144-9.
    • (1995) Nat Genet , vol.11 , pp. 144-149
    • Bourgeron, T.1    Rustin, P.2    Chretien, D.3    Birch-Machin, M.4    Bourgeois, M.5    Viegas-Pequignot, E.6
  • 14
    • 0000376151 scopus 로고
    • Subacute necrotizing encephalomyelopathy in an infant
    • Leigh D. Subacute necrotizing encephalomyelopathy in an infant. J Neurol Neurosurg Psychiatr 1951;14:216-21.
    • (1951) J Neurol Neurosurg Psychiatr , vol.14 , pp. 216-221
    • Leigh, D.1
  • 16
    • 18344381765 scopus 로고    scopus 로고
    • Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic patients with head and neck paragangliomas
    • Baysal B, Willett-Brozick J, Lawrence E, Drovdlic C, Savul S, McLeod D, et al. Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic patients with head and neck paragangliomas. J Med Genet 2002;39:178-83.
    • (2002) J Med Genet , vol.39 , pp. 178-183
    • Baysal, B.1    Willett-Brozick, J.2    Lawrence, E.3    Drovdlic, C.4    Savul, S.5    McLeod, D.6
  • 18
    • 0037594892 scopus 로고    scopus 로고
    • Autosomal dominant malignant and catecholamine-producing paraganglioma caused by a splice donor site mutation in SDHC
    • Niemann S, Muller U, Engelhardt D, Lohse P. Autosomal dominant malignant and catecholamine-producing paraganglioma caused by a splice donor site mutation in SDHC. Hum Genet 2003;113:92-4.
    • (2003) Hum Genet , vol.113 , pp. 92-94
    • Niemann, S.1    Muller, U.2    Engelhardt, D.3    Lohse, P.4
  • 20
    • 0037422207 scopus 로고    scopus 로고
    • Novel succinate dehydrogenase subunit B (SDHB) mutations in familial phaeochromocytomas and paragangliomas, but an absence of somatic SDHB mutations in sporadic phaeochromocytomas
    • Benn DE, Croxson MS, Tucker K, Bambach CP, Richardson AL, Delbridge L, et al. Novel succinate dehydrogenase subunit B (SDHB) mutations in familial phaeochromocytomas and paragangliomas, but an absence of somatic SDHB mutations in sporadic phaeochromocytomas. Oncogene 2003;22:1358-64.
    • (2003) Oncogene , vol.22 , pp. 1358-1364
    • Benn, D.E.1    Croxson, M.S.2    Tucker, K.3    Bambach, C.P.4    Richardson, A.L.5    Delbridge, L.6
  • 21
    • 0034964421 scopus 로고    scopus 로고
    • Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial phaeochromocytoma and to familial paraganglioma
    • Astuti D, Latif F, Dallol A, Dahia PL, Douglas F, George E, et al. Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial phaeochromocytoma and to familial paraganglioma. Am J Hum Genet 2001;69:49-54.
    • (2001) Am J Hum Genet , vol.69 , pp. 49-54
    • Astuti, D.1    Latif, F.2    Dallol, A.3    Dahia, P.L.4    Douglas, F.5    George, E.6
  • 22
    • 0037307412 scopus 로고    scopus 로고
    • A novel mutation in the SDHD gene in a family with inherited paragangliomas - Implications of genetic diagnosis for follow up and treatment
    • Renard L, Godfraind C, Boon LM, Vikkula M. A novel mutation in the SDHD gene in a family with inherited paragangliomas - implications of genetic diagnosis for follow up and treatment. Head Neck 2003;25:146-51.
    • (2003) Head Neck , vol.25 , pp. 146-151
    • Renard, L.1    Godfraind, C.2    Boon, L.M.3    Vikkula, M.4
  • 23
    • 0033767445 scopus 로고    scopus 로고
    • Mutations in SDHC cause autosomal dominant paraganglioma, type 3
    • Niemann S, Muller U. Mutations in SDHC cause autosomal dominant paraganglioma, type 3. Nat Genet 2000;26:268-70.
    • (2000) Nat Genet , vol.26 , pp. 268-270
    • Niemann, S.1    Muller, U.2
  • 24
    • 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
    • Gimenez-Roqueplo AP, Favier J, Rustin P, Mourad JJ, Plouin PF, Corvol P, et al. 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. Am J Hum Genet 2001;69:1186-97.
    • (2001) Am J Hum Genet , vol.69 , 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
  • 25
    • 0027263149 scopus 로고
    • Purification and crystallization of fumarase C from Escherichia coli
    • Weaver TM, Levitt DG, Banaszak LJ. Purification and crystallization of fumarase C from Escherichia coli. J Mol Biol 1993;231:141-4.
    • (1993) J Mol Biol , vol.231 , pp. 141-144
    • Weaver, T.M.1    Levitt, D.G.2    Banaszak, L.J.3
  • 27
    • 0029854921 scopus 로고    scopus 로고
    • Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli
    • Weaver T, Banaszak L. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry 1996;35:13955-65.
    • (1996) Biochemistry , vol.35 , pp. 13955-13965
    • Weaver, T.1    Banaszak, L.2
  • 28
    • 0033610885 scopus 로고    scopus 로고
    • Pig heart fumarase contains two distinct substrate-binding sites differing in affinity
    • Beeckmans S, Van Driessche E. Pig heart fumarase contains two distinct substrate-binding sites differing in affinity. J Biol Chem 1998;273:31661-9.
    • (1998) J Biol Chem , vol.273 , pp. 31661-31669
    • Beeckmans, S.1    Van Driessche, E.2
  • 30
    • 0034059135 scopus 로고    scopus 로고
    • Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome
    • Parfait B, Chretien D, Rotig A, Marsac C, Munnich A, Rustin P. Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome. Hum Genet 2000;106:236-43.
    • (2000) Hum Genet , vol.106 , pp. 236-243
    • Parfait, B.1    Chretien, D.2    Rotig, A.3    Marsac, C.4    Munnich, A.5    Rustin, P.6
  • 31
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 alpha is required for solid tumor formation and embryonic vascularization
    • Ryan HE, Lo J, Johnson RS. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J 1998;17:3005-15.
    • (1998) EMBO J , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 32
    • 0031445126 scopus 로고    scopus 로고
    • Von Hippel-Lindau disease
    • Baltimore
    • Maher ER, Kaelin WG, Jr. von Hippel-Lindau disease. Medicine (Baltimore) 1997;76:381-91.
    • (1997) Medicine , vol.76 , pp. 381-391
    • Maher, E.R.1    Kaelin Jr., W.G.2
  • 33
    • 0034682783 scopus 로고    scopus 로고
    • Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein
    • Cockman ME, Masson N, Mole DR, Jaakkola P, Chang GW, Clifford SC, et al. Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein. J Biol Chem 2000;275:25733-41.
    • (2000) J Biol Chem , vol.275 , pp. 25733-25741
    • Cockman, M.E.1    Masson, N.2    Mole, D.R.3    Jaakkola, P.4    Chang, G.W.5    Clifford, S.C.6
  • 35
    • 0035339044 scopus 로고    scopus 로고
    • Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumorigenesis in von Hippel-Lindau disease
    • Clifford SC, Cockman ME, Smallwood AC, Mole DR, Woodward ER, Maxwell PH, et al. Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumorigenesis in von Hippel-Lindau disease. Hum Mol Genet 2001;10:1029-38.
    • (2001) Hum Mol Genet , vol.10 , pp. 1029-1038
    • Clifford, S.C.1    Cockman, M.E.2    Smallwood, A.C.3    Mole, D.R.4    Woodward, E.R.5    Maxwell, P.H.6
  • 36
    • 0035336706 scopus 로고    scopus 로고
    • Von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF
    • Hoffman MA, Ohh M, Yang H, Klco JM, Ivan M, Kaelin WG, Jr. von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF. Hum Mol Genet 2001;10:1019-27.
    • (2001) Hum Mol Genet , vol.10 , pp. 1019-1027
    • Hoffman, M.A.1    Ohh, M.2    Yang, H.3    Klco, J.M.4    Ivan, M.5    Kaelin Jr., W.G.6
  • 37
    • 0035211640 scopus 로고    scopus 로고
    • Quantification of vascular endothelial growth factor-A in leiomyomas and adjacent myometrium
    • Lond
    • Gentry CC, Okolo SO, Fong LF, Crow JC, Maclean AB, Perrett CW. Quantification of vascular endothelial growth factor-A in leiomyomas and adjacent myometrium. Clin Sci (Lond) 2001;101:691-5.
    • (2001) Clin Sci , vol.101 , pp. 691-695
    • Gentry, C.C.1    Okolo, S.O.2    Fong, L.F.3    Crow, J.C.4    Maclean, A.B.5    Perrett, C.W.6
  • 38
    • 0036295999 scopus 로고    scopus 로고
    • Insights from gene arrays on the development and growth regulation of uterine leiomyomata
    • Tsibris JC, Segars J, Coppola D, Mane S, Wilbanks GD, O'Brien WF, et al. Insights from gene arrays on the development and growth regulation of uterine leiomyomata. Fertil Steril 2002;78:114-21.
    • (2002) Fertil Steril , vol.78 , pp. 114-121
    • Tsibris, J.C.1    Segars, J.2    Coppola, D.3    Mane, S.4    Wilbanks, G.D.5    O'Brien, W.F.6
  • 39
    • 0036006511 scopus 로고    scopus 로고
    • Bcl-2 family members and functional electron transport chain regulate oxygen deprivation-induced cell death
    • McClintock DS, Santore MT, Lee VY, Brunelle J, Budinger GR, Zong WX, et al. Bcl-2 family members and functional electron transport chain regulate oxygen deprivation-induced cell death. Mol Cell Biol 2002;22:94-104.
    • (2002) Mol Cell Biol , vol.22 , pp. 94-104
    • McClintock, D.S.1    Santore, M.T.2    Lee, V.Y.3    Brunelle, J.4    Budinger, G.R.5    Zong, W.X.6
  • 40
    • 0037364314 scopus 로고    scopus 로고
    • A role for mitochondrial enzymes in inherited neoplasia and beyond
    • Eng C, Kiuru M, Fernandez MJ, Aaltonen LA. A role for mitochondrial enzymes in inherited neoplasia and beyond. Nat Rev Cancer 2003;3:193-202.
    • (2003) Nat Rev Cancer , vol.3 , pp. 193-202
    • Eng, C.1    Kiuru, M.2    Fernandez, M.J.3    Aaltonen, L.A.4
  • 41
    • 0036130362 scopus 로고    scopus 로고
    • Glutamine and its relationship with intracellular redox status, oxidative stress and cell proliferation/death
    • Mates JM, Perez-Gomez C, Nunez de Castro I, Asenjo M, Marquez J. Glutamine and its relationship with intracellular redox status, oxidative stress and cell proliferation/death. Int J Biochem Cell Biol 2002;34:439-58.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 439-458
    • Mates, J.M.1    Perez-Gomez, C.2    Nunez De Castro, I.3    Asenjo, M.4    Marquez, J.5
  • 42
    • 17644448326 scopus 로고
    • Amplification of glutamate-induced oxidative stress
    • Savolainen KM, Loikkanen J, Naarala J. Amplification of glutamate-induced oxidative stress. Toxicol Lett 1995;82-3:399-405.
    • (1995) Toxicol Lett , vol.82 , Issue.3 , pp. 399-405
    • Savolainen, K.M.1    Loikkanen, J.2    Naarala, J.3
  • 43
    • 0032570704 scopus 로고    scopus 로고
    • Glucose deprivation-induced cytotoxicity and alterations in mitogen-activated protein kinase activation are mediated by oxidative stress in multidrug-resistant human breast carcinoma cells
    • Lee YJ, Galoforo SS, Berns CM, Chen JC, Davis BH, Sim JE, et al. Glucose deprivation-induced cytotoxicity and alterations in mitogen-activated protein kinase activation are mediated by oxidative stress in multidrug-resistant human breast carcinoma cells. J Biol Chem 1998;273:5294-9.
    • (1998) J Biol Chem , vol.273 , pp. 5294-5299
    • Lee, Y.J.1    Galoforo, S.S.2    Berns, C.M.3    Chen, J.C.4    Davis, B.H.5    Sim, J.E.6
  • 44
    • 0036051315 scopus 로고    scopus 로고
    • Glutamine protects activated human T cells from apoptosis by upregulating glutathione and Bcl-2 levels
    • Chang WK, Yang KD, Chuang H, Jan JT, Shaio MF. Glutamine protects activated human T cells from apoptosis by upregulating glutathione and Bcl-2 levels. Clin Immunol 2002;104:151-60.
    • (2002) Clin Immunol , vol.104 , pp. 151-160
    • Chang, W.K.1    Yang, K.D.2    Chuang, H.3    Jan, J.T.4    Shaio, M.F.5
  • 46
    • 0036062729 scopus 로고    scopus 로고
    • Succinate dehydrogenase and human diseases: New insights into a well-known enzyme
    • Rustin P, Munnich A, Rotig A. Succinate dehydrogenase and human diseases: new insights into a well-known enzyme. Eur J Hum Genet 2002;10:289-91.
    • (2002) Eur J Hum Genet , vol.10 , pp. 289-291
    • Rustin, P.1    Munnich, A.2    Rotig, A.3
  • 47
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster L, Dallner G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim Biophys Acta 1995;1271:195-204.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 48
    • 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, et al. A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans. J Biol Chem 2001;276:41553-8.
    • (2001) J Biol Chem , vol.276 , pp. 41553-41558
    • Senoo-Matsuda, N.1    Yasuda, K.2    Tsuda, M.3    Ohkubo, T.4    Yoshimura, S.5    Nakazawa, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.