Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolism

Reitman, Z. J.; Yan, H.

doi:10.1093/jnci/djq187

Cited by 567Cancer, Hypoxia, and MetabolismGlioma Diagnosis and TreatmentBiochemical Acid Research Studies

Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolism

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Reitman, Z. J., Yan, H.·2010·JNCI Journal of the National Cancer Institute

DOI 10.1093/jnci/djq187PMC PMC2897878

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Abstract

Dysregulation of metabolism is a common phenomenon in cancer cells. The NADP(+)-dependent isocitrate dehydrogenases 1 and 2 (IDH1 and IDH2) function at a crossroads of cellular metabolism in lipid synthesis, cellular defense against oxidative stress, oxidative respiration, and oxygen-sensing signal transduction. We review the normal functions of the encoded enzymes, frequent mutations of IDH1 and IDH2 recently found in human cancers, and possible roles for the mutated enzymes in human disease. IDH1 and IDH2 mutations occur frequently in some types of World Health Organization grades 2-4 gliomas and in acute myeloid leukemias with normal karyotype. IDH1 and IDH2 mutations are remarkably specific to codons that encode conserved functionally important arginines in the active site of each enzyme. To date, all IDH1 mutations have been identified at the Arg132 codon. Mutations in IDH2 have been identified at the Arg140 codon, as well as at Arg172, which is aligned with IDH1 Arg132. IDH1 and IDH2 mutations are usually heterozygous in cancer, and they appear to confer a neomorphic enzyme activity for the enzymes to catalyze the production of D-2-hydroxyglutarate. Study of alterations in these metabolic enzymes may provide insights into the metabolism of cancer cells and uncover novel avenues for development of anticancer therapeutics.

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Metabolic reprogramming is a hallmark of cancer based on the discovery of mutations and alterations in IDH1 and IDH2 along with SDH, FH, and PKM2.
“There is a renewed interest in the area of cancer metabolism with metabolic reprogramming coined as a hallmark of cancer based on the discovery of mutations and alterations in IDH1 and IDH2 along with succinate dehydrogenase (SDH), fumarate hydratase (FH), and pyruvate kinase M2 (PKM2) [41, 42].”
From Modeling APC mutagenesis and familial adenomatous polyposis using human iPS cells (2018) · cites this paper as [42]
The opening summary (page not specified in our copy) says metabolic dysregulation is common in cancer and reports frequent IDH1 and IDH2 mutations in certain cancers. It does not establish that metabolic reprogramming was designated a cancer hallmark on the basis of the full list of enzymes. SDH and FH appear in a cited reference, while the searched passages do not substantiate the PKM2 part of the claim. (LLM, conf=0.85)
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UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
The 2007 WHO Classification of Tumours of the Central Nervous System
Louis, D. N., Ohgaki, H., Wiestler, O. D., Cavenee, W. K., Burger, P. C., Jouvet, A., Scheithauer, B. W., & Kleihues, P. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0243-4 · Cited by 15,422 · see citing works
An Integrated Genomic Analysis of Human Glioblastoma Multiforme
Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857 · see citing works
Self-citation
IDH1 and IDH2 Mutations in Gliomas
Yan, H., Parsons, D. W., Jin, G., McLendon, R., Rasheed, B. A., Yuan, W., Kos, I., Batinic-Haberle, I., Jones, S., Riggins, G. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808710 · Cited by 5,847 · see citing works
Self-citation
Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154 · see citing works
The Consensus Coding Sequences of Human Breast and Colorectal Cancers
Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161 · see citing works
Recurring mutations found by sequencing an acute myeloid leukemia genome
Mardis, E. R., Ding, L., Dooling, D. J., Larson, D. E., McLellan, M. D., Chen, K., Koboldt, D. C., Fulton, R. S., Delehaunty, K. D., McGrath, S. D., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0903840 · Cited by 2,219 · see citing works
The Common Feature of Leukemia-Associated IDH1 and IDH2 Mutations Is a Neomorphic Enzyme Activity Converting α-Ketoglutarate to 2-Hydroxyglutarate
Ward, P. S., Patel, J., Wise, D. R., Abdel-Wahab, O., Bennett, B. D., Coller, H. A., Cross, J. R., Fantin, V. R., Hedvat, C. V., Perl, A. E., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.01.020 · Cited by 2,020 · see citing works
Type and frequency of IDH1 and IDH2 mutations are related to astrocytic and oligodendroglial differentiation and age: a study of 1,010 diffuse gliomas
Hartmann, C. J., Meyer, J., Balß, J., Capper, D., Mueller, W. C., Christians, A., Felsberg, J., Wolter, M., Mawrin, C., Wick, W., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0561-9 · Cited by 1,163 · see citing works
Glioma-Derived Mutations in IDH1 Dominantly Inhibit IDH1 Catalytic Activity and Induce HIF-1α
Zhao, S., Lin, Y., Xu, W., Jiang, W., Zha, Z., Wang, P., Yu, W., Li, Z., Gong, L., Peng, Y., et al. (2009) · Science · doi:10.1126/science.1170944 · Cited by 1,119 · see citing works
Analysis of the IDH1 codon 132 mutation in brain tumors
Balss, J., Meyer, J., Mueller, W., Korshunov, A., Hartmann, C., & von Deimling, A. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0455-2 · Cited by 1,036 · see citing works
IDH1 mutations are early events in the development of astrocytomas and oligodendrogliomas
Watanabe, T., Nobusawa, S., Kleihues, P., & Ohgaki, H. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080958 · Cited by 1,027 · see citing works
Isocitrate Dehydrogenase 1 Codon 132 Mutation Is an Important Prognostic Biomarker in Gliomas
Sanson, M., Marie, Y., Paris, S., Idbaïh, A., Laffaire, J., Ducray, F., Hallani, S. E., Boisselier, B., Mokhtari, K., Hoang‐Xuan, K., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2009.21.9832 · Cited by 1,007 · see citing works
Cancer-associated metabolite 2-hydroxyglutarate accumulates in acute myelogenous leukemia with isocitrate dehydrogenase 1 and 2 mutations
Gross, S., Cairns, R. A., Minden, M. D., Driggers, E. M., Bittinger, M. A., Jang, H. G., Sasaki, M., Jin, S., Schenkein, D. P., Su, S. M., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20092506 · Cited by 736 · see citing works
IDH1 Mutations as Molecular Signature and Predictive Factor of Secondary Glioblastomas
Nobusawa, S., Watanabe, T., Kleihues, P., & Ohgaki, H. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-0715 · Cited by 707 · see citing works
Succinate dehydrogenase and fumarate hydratase: linking mitochondrial dysfunction and cancer
King, A., Selak, M. A., & Gottlieb, E. (2006) · Oncogene · doi:10.1038/sj.onc.1209594 · Cited by 672 · see citing works
MOLECULAR PATHOLOGY OF MALIGNANT GLIOMAS
Louis, D. N. (2006) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.1.110304.100043 · Cited by 647 · see citing works
IDH1 mutations are present in the majority of common adult gliomas but rare in primary glioblastomas
Ichimura, K., Pearson, D. M., Kocialkowski, S., Bäcklund, L. M., Chan, R., Jones, D., & Collins, V. P. (2009) · Neuro-Oncology · doi:10.1215/15228517-2009-025 · Cited by 593 · see citing works
Genetic alterations and signaling pathways in the evolution of gliomas
Ohgaki, H., & Kleihues, P. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01308.x · Cited by 452 · see citing works
Cytosolic NADP+-dependent isocitrate dehydrogenase status modulates oxidative damage to cells
Lee, S. M., Koh, H., Park, D., Song, B. J., Huh, T., & Park, J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00815-8 · Cited by 422 · see citing works
Structures of Human Cytosolic NADP-dependent Isocitrate Dehydrogenase Reveal a Novel Self-regulatory Mechanism of Activity
Xu, X., Zhao, J., Xu, Z., Peng, B., Huang, Q., Arnold, E., & Ding, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404298200 · Cited by 407 · see citing works
IDH1mutations at residue p.R132 (IDH1R132) occur frequently in high-grade gliomas but not in other solid tumors
Bleeker, F. E., Lamba, S., Leenstra, S., Troost, D., Hulsebos, T. J. M., Vandertop, W. P., Frattini, M., Molinari, F., Knowles, M. A., Cerrato, A., et al. (2009) · Human Mutation · doi:10.1002/humu.20937 · Cited by 365 · see citing works
The Tricarboxylic Acid Cycle, an Ancient Metabolic Network with a Novel Twist
Mailloux, R. J., Bériault, R., Lemire, J. A., Singh, R., Chénier, D., Hamel, R. D., & Appanna, V. D. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000690 · Cited by 329 · see citing works
Mutational analysis of IDH1 codon 132 in glioblastomas and other common cancers
Kang, M. R., Kim, M. S., Oh, J. E., Kim, Y. R., Song, S. Y., Seo, S. I., Lee, J. Y., Yoo, N. J., & Lee, S. H. (2009) · International Journal of Cancer · doi:10.1002/ijc.24379 · Cited by 312 · see citing works
The prognostic IDH1 R132 mutation is associated with reduced NADP+-dependent IDH activity in glioblastoma
Bleeker, F. E., Atai, N. A., Lamba, S., Jonker, A., Rijkeboer, D., Bosch, K. S., Tigchelaar, W., Troost, D., Vandertop, W. P., Bardelli, A., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0645-6 · Cited by 304 · see citing works
Somatic Mutations ofIDH1andIDH2in the Leukemic Transformation of Myeloproliferative Neoplasms
Green, A. R., & Beer, P. A. (2010) · New England Journal of Medicine · doi:10.1056/nejmc0910063 · Cited by 285 · see citing works
Combined molecular analysis of BRAF and IDH1 distinguishes pilocytic astrocytoma from diffuse astrocytoma
Korshunov, A., Meyer, J., Capper, D., Christians, A., Remke, M., Witt, H., Pfister, S. M., von Deimling, A., & Hartmann, C. J. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0550-z · Cited by 274 · see citing works
Cytosolic NADP+-dependent Isocitrate Dehydrogenase Plays a Key Role in Lipid Metabolism
Koh, H., Lee, S., Son, B.-G., Lee, S.-H., Ryoo, Z. Y., Chang, K., Park, J., Park, D., Song, B. J., Veech, R. L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402260200 · Cited by 253 · see citing works
Regulation of an Enzyme by Phosphorylation at the Active Site
Hurley, J. H., Dean, A. M., Sohl, J. L., Koshland, D. E., & Stroud, R. M. (1990) · Science · doi:10.1126/science.2204109 · Cited by 249 · see citing works
A Pyruvate Cycling Pathway Involving Cytosolic NADP-dependent Isocitrate Dehydrogenase Regulates Glucose-stimulated Insulin Secretion
Ronnebaum, S. M., Ilkayeva, O., Burgess, S. C., Joseph, J. W., Lu, D., Stevens, R. D., Becker, T. C., Sherry, A. D., Newgard, C. B., & Jensen, M. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511908200 · Cited by 230 · see citing works
Metabolic enzymes as oncogenes or tumor suppressors
Thompson, C. B. (2009) · New England Journal of Medicine · doi:10.1056/nejme0810213 · Cited by 213 · see citing works
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Hurley, J. H., Thorsness, P. E., Ramalingam, V., Helmers, N. S., Koshland, D. E., & Stroud, R. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.8635 · Cited by 207 · see citing works
Proton‐translocating transhydrogenase and NAD‐ and NADP‐linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria
Sazanov, L. A., & Jackson, J. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00370-x · Cited by 205 · see citing works
The Human PICD Gene Encodes a Cytoplasmic and Peroxisomal NADP+-dependent Isocitrate Dehydrogenase
Geisbrecht, B. V., & Gould, S. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30527 · Cited by 189 · see citing works
Thioredoxin and Its Related Molecules: Update 2005
Nakamura, H. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.823 · Cited by 185 · see citing works
Insights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycle
Hartong, D. T., Dange, M., McGee, T. L., Berson, E. L., Dryja, T. P., & Colman, R. F. (2008) · Nature Genetics · doi:10.1038/ng.223 · Cited by 172 · see citing works
Function and expression of yeast mitochondrial NAD- and NADP-specific isocitrate dehydrogenases
Haselbeck, R. J., & McAlister-Henn, L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50315-5 · Cited by 160 · see citing works
The Mitochondrial Citrate/Isocitrate Carrier Plays a Regulatory Role in Glucose-stimulated Insulin Secretion
Joseph, J. W., Jensen, M. V., Ilkayeva, O., Palmieri, F., Alarcón, C., Rhodes, C. J., & Newgard, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602606200 · Cited by 160 · see citing works
Peroxisomal β‐oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions
van Roermund, C. W. T., Hettema, E. H., Kal, A. J., van den Berg, M., Tabak, H. F., & Wanders, R. J. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.3.677 · Cited by 148 · see citing works
Cytochrome P-450 Polymorphisms and Response to Clopidogrel
Taubert, D., Bouman, H. J., & van Werkum, J. W. (2009) · New England Journal of Medicine · doi:10.1056/nejmc090391 · Cited by 135 · see citing works
IDH1andIDH2Mutations in Gliomas
Carli, E. D., Wang, X.-W., & Puget, S. (2009) · New England Journal of Medicine · doi:10.1056/nejmc090593 · Cited by 134 · see citing works
Inactivation of NADP+-dependent Isocitrate Dehydrogenase by Peroxynitrite
Lee, J. H., Yang, E. S., & Park, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302332200 · Cited by 132 · see citing works
Electrostatic and Steric Contributions to Regulation at the Active Site of Isocitrate Dehydrogenase
Dean, A. M., & Koshland, D. E. (1990) · Science · doi:10.1126/science.2204110 · Cited by 120 · see citing works
Crystal Structure of Porcine Mitochondrial NADP+-dependent Isocitrate Dehydrogenase Complexed with Mn2+ and Isocitrate
Ceccarelli, C., Grodsky, N. B., Ariyaratne, N., Colman, R. F., & Bahnson, B. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207306200 · Cited by 116 · see citing works
Multiple NADPH-producing pathways control glutathione (GSH) content in retina
Winkler, B. S., Desantis, N. M., & Solomon, F. (1986) · Experimental Eye Research · doi:10.1016/s0014-4835(86)80013-6 · Cited by 106 · see citing works
IDH1 gene transcription is sterol regulated and activated by SREBP-1a and SREBP-2 in human hepatoma HepG2 cells
Shechter, I., Dai, P., Huo, L., & Guan, G. (2003) · Journal of Lipid Research · doi:10.1194/jlr.m300285-jlr200 · Cited by 101 · see citing works
IDP3 Encodes a Peroxisomal NADP-dependent Isocitrate Dehydrogenase Required for the β-Oxidation of Unsaturated Fatty Acids
Henke, B., Girzalsky, W., Berteaux‐Lecellier, V., & Erdmann, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3702 · Cited by 94 · see citing works
Selective acquisition of IDH1 R132C mutations in astrocytomas associated with Li-Fraumeni syndrome
Watanabe, T., Vital, A., Nobusawa, S., Kleihues, P., & Ohgaki, H. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0528-x · Cited by 93 · see citing works
Regulation of Ionizing Radiation-induced Apoptosis by Mitochondrial NADP+-dependent Isocitrate Dehydrogenase
Lee, J. H., Kim, S. Y., Kil, I. S., & Park, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700303200 · Cited by 89 · see citing works
REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME
Hurley, J. H., Dean, A. M., Thorsness, P. E., Koshland, D. E., & Stroud, R. M. (1989) · Worldwide Protein Data Bank · doi:10.2210/pdb4icd/pdb · Cited by 84 · see citing works
Comparative Proteomic Analysis of Brains of Naturally Aging Mice
Yang, S., Liu, T., Li, S., Zhang, X., Ding, Q., Que, H., Yan, X., Wei, K., & Liu, S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.04.012 · Cited by 82 · see citing works
Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family
Nekrutenko, A., Hillis, D. M., Patton, J. C., Bradley, R. D., & Baker, R. J. (1998) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a025894 · Cited by 80 · see citing works
Kinetic mechanism of Escherichia coli isocitrate dehydrogenase
Dean, A. M., & Koshland, D. E. (1993) · Biochemistry · doi:10.1021/bi00087a007 · Cited by 80 · see citing works
Activity of purified NAD-specific isocitrate dehydrogenase at modulator and substrate concentrations approximating conditions in mitochondria
Gabriel, J. L., Zervos, P. R., & Plaut, G. W. E. (1986) · Metabolism · doi:10.1016/0026-0495(86)90175-7 · Cited by 79 · see citing works
Inactivation of NADP+-dependent isocitrate dehydrogenase by nitric oxide
Yang, E. S., Richter, C., Chun, J., Huh, T., Kang, S., & Park, J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00981-4 · Cited by 76 · see citing works
Phosphorylation Inactivates Escherichia coli Isocitrate Dehydrogenase by Preventing Isocitrate Binding
Dean, A. M., Lee, M. H. I., & Koshland, D. E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47087-7 · Cited by 75 · see citing works
Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme.
Hurley, J. H., Dean, A. M., Thorsness, P. E., Koshland, D. E., & Stroud, R. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39632-2 · Cited by 75 · see citing works
Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria
Kranendijk, M., Struys, E. A., Gibson, K. M., Wickenhagen, W. V., Abdenur, J. E., Buechner, J., Christensen, E., de Kremer, R. D., Errami, A., Gissen, P., et al. (2009) · Human Mutation · doi:10.1002/humu.21186 · Cited by 74 · see citing works
IDH1 and IDH2: Not Your Typical Oncogenes
Reitman, Z. J., Parsons, D. W., & Yan, H. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.02.024 · Cited by 73 · see citing works
Self-citation
L -2-Hydroxyglutaric Aciduria and Brain Tumors in Children with Mutations in the L2HGDH Gene: Neuroimaging Findings
Haliloğlu, G., Jobard, F., Oguz, K., Anlar, B., Akalan, N., Coşkun, T., Sass, J. O., Fischer, J., & Topcu, M. (2008) · Neuropediatrics · doi:10.1055/s-2008-1081217 · Cited by 69 · see citing works
Reverse flux through cardiac NADP+-isocitrate dehydrogenase under normoxia and ischemia
Comte, B., Vincent, G., Bouchard, B., Benderdour, M., & Rosiers, C. D. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00287.2002 · Cited by 67 · see citing works
IDH1 Mutations in Gliomas: When an Enzyme Loses Its Grip
Frezza, C., Tennant, D. A., & Gottlieb, E. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.031 · Cited by 66 · see citing works
Dependence of Peroxisomal β-Oxidation on Cytosolic Sources of NADPH
Minard, K. I., & McAlister-Henn, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3402 · Cited by 66 · see citing works
Cytosolic NADP(+)-dependent isocitrate dehydrogenase. Isolation of rat cDNA and study of tissue-specific and developmental expression of mRNA.
Jennings, G., Sechi, S., Stevenson, P. M., Tuckey, R. C., Parmelee, D. C., & McAlister-Henn, L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31629-0 · Cited by 66 · see citing works
Role of NADP+‐dependent isocitrate dehydrogenase (NADP+‐ICDH) on cellular defence against oxidative injury byγ‐rays
Lee, S. ‐., Jo, S., Lee, S. ‐., Koh, H., Song, H.-S., Park, J., Lee, W. H., & Huh, T. L. (2004) · International Journal of Radiation Biology · doi:10.1080/09553000400007680 · Cited by 63 · see citing works
Regulation of singlet oxygen-induced apoptosis by cytosolic NADP+-dependent isocitrate dehydrogenase
Kim, S.-Y., Lee, S. M., Tak, J. K., Choi, K. S., Kwon, T. K., & Park, J. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9421-x · Cited by 61 · see citing works
Localization of Cytosolic NADP-dependent Isocitrate Dehydrogenase in the Peroxisomes of Rat Liver Cells
Yoshihara, T., Hamamoto, T., Munakata, R., Tajiri, R., Ohsumi, M., & Yokota, S. (2001) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540104900906 · Cited by 58 · see citing works
Cellular Defense against UVB-Induced Phototoxicity by Cytosolic NADP+-Dependent Isocitrate Dehydrogenase
Jo, S., Lee, S.-H., Chun, H., Lee, S. M., Koh, H., Lee, S., Chun, J., Park, J., & Huh, T. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6667 · Cited by 56 · see citing works
Inactivation of NADP+-dependent isocitrate dehydrogenase by reactive oxygen species
Lee, S. M., Huh, T., & Park, J. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01351-7 · Cited by 52 · see citing works
Small interfering RNA-mediated silencing of mitochondrial NADP+-dependent isocitrate dehydrogenase enhances the sensitivity of HeLa cells toward tumor necrosis factor-α and anticancer drugs
Kil, I. S., Kim, S. Y., Lee, S. J., & Park, J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.07.009 · Cited by 51 · see citing works
Glycation-induced inactivation of NADP+-dependent isocitrate dehydrogenase: implications for diabetes and aging
Kil, I. S., Lee, J. H., Shin, A. H., & Park, J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.025 · Cited by 44 · see citing works
Inactivation of NADP+-dependent Isocitrate Dehydrogenase by Lipid Peroxidation Products
Yang, J.-H., Yang, E. S., & Park, J. (2004) · Free Radical Research · doi:10.1080/10715760310001657712 · Cited by 42 · see citing works
Identification by Mutagenesis of Arginines in the Substrate Binding Site of the Porcine NADP-dependent Isocitrate Dehydrogenase
Soundar, S., Danek, B. L., & Colman, R. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5606 · Cited by 38 · see citing works
Expression and Mutagenesis of Mammalian Cytosolic NADP+-Specific Isocitrate Dehydrogenase
Jennings, G. T., Minard, K. I., & McAlister-Henn, L. (1997) · Biochemistry · doi:10.1021/bi970916r · Cited by 32 · see citing works
Novel insights into L ‐2‐hydroxyglutaric aciduria: Mass isotopomer studies reveal 2‐oxoglutaric acid as the metabolic precursor of L ‐2‐hydroxyglutaric acid
Struys, E. A., Gibson, K. M., & Jakobs, C. (2007) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-007-0697-5 · Cited by 30 · see citing works
An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation
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Yang, E. S., Lee, J. H., & Park, J. (2008) · Biochimie · doi:10.1016/j.biochi.2008.03.001 · Cited by 25 · see citing works
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Lee, S., Park, S. Y., Shin, S., Kil, I. S., Yang, E. S., & Park, J. (2009) · Free Radical Research · doi:10.1080/10715760802653661 · Cited by 20 · see citing works
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Park, S. W., Chung, N. G., Han, J. Y., Eom, H., Lee, J. Y., Yoo, N. J., & Lee, S. H. (2009) · International Journal of Cancer · doi:10.1002/ijc.24647 · Cited by 19 · see citing works
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Shin, S., Kil, I. S., & Park, J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.067 · Cited by 18 · see citing works
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Broughton, S. J., Kane, N. S., Arthur, B. I., Yoder, M., Greenspan, R. J., & Robichon, A. (1996) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19960315)60:4 · Cited by 18 · see citing works
Inactivation of mitochondrial NADP+-dependent isocitrate dehydrogenase by hypochlorous acid
Park, S. Y., Lee, S., Shin, S., & Park, J. (2008) · Free Radical Research · doi:10.1080/10715760802098834 · Cited by 17 · see citing works
Modulation of NADP+-dependent isocitrate dehydrogenase in aging
Kil, I. S., Lee, Y. S., Bae, Y., Huh, T. L., & Park, J. (2004) · Redox Report · doi:10.1179/135100004225006056 · Cited by 15 · see citing works
Inactivation of NADP+-dependent isocitrate dehydrogenase by singlet oxygen derived from photoactivated rose bengal
Kim, S.-Y., Tak, J. K., & Park, J. (2004) · Biochimie · doi:10.1016/j.biochi.2004.08.001 · Cited by 15 · see citing works
Glutathionylation regulates cytosolic NADP+-dependent isocitrate dehydrogenase activity
Shin, S., Shin, S., Oh, C. J., Kil, I. S., & Park, J. (2009) · Free Radical Research · doi:10.1080/10715760902801525 · Cited by 15 · see citing works

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2 of the 88 references couldn’t be matched to a known paper.

Research works printed but not linked: 4

[7]7. Luo H, Shan X, Wu J. Expression of human mitochondrial NADPdependent isocitrate dehydrogenase during lymphocyte activation. J Cell Biochem. 1996;60(4):495-507.
[67]67. De Carli E, Wang X, Puget S. IDH1 and IDH2 mutations in gliomas. N Engl J Med. 2009;360(21):2248;author reply 2249.
[68]68. Reitman Z, Yan H. IDH1 and IDH2 mutations in gliomas. N Engl J Med. 2009;360(21):2249;author reply 2249.
[84]84. Ducray F, Marie Y, Sanson M. IDH1 and IDH2 mutations in gliomas. N Engl J Med. 2009;360(21):2248;author reply 2249.

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Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works
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The Orphan Nuclear Receptor NR4A1 (Nur77) Regulates Oxidative and Endoplasmic Reticulum Stress in Pancreatic Cancer Cells
Lee, S., Jin, U.-H., Kang, J. H., Kim, S. B., Guthrie, A. S., Sreevalsan, S., Lee, J., & Safe, S. H. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0567 · Cited by 109 · see citing works
Isocitrate dehydrogenase inhibitors in acute myeloid leukemia
Liu, X., & Gong, Y. (2019) · Biomarker Research · doi:10.1186/s40364-019-0173-z · Cited by 109 · see citing works
Molecular pathology in adult high‐grade gliomas: from molecular diagnostics to target therapies
Masui, K., Cloughesy, T. F., & Mischel, P. S. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01238.x · Cited by 107 · see citing works
The Role of Mitochondrial NADPH-Dependent Isocitrate Dehydrogenase in Cancer Cells
Smolková, K., & Ježek, P. (2012) · International Journal of Cell Biology · doi:10.1155/2012/273947 · Cited by 108 · see citing works
Reductive carboxylation epigenetically instructs T cell differentiation
Jaccard, A., Wyss, T., Maldonado‐Pérez, N., Rath, J. A., Bevilacqua, A., Peng, J.-J., Lepez, A., Gunten, C. V., Franco, F., Kao, K., et al. (2023) · Nature · doi:10.1038/s41586-023-06546-y · Cited by 104 · see citing works
Mutational landscape of AML with normal cytogenetics: Biological and clinical implications
Martelli, M. P., Sportoletti, P., Tiacci, E., Martelli, M. F., & Falini, B. (2012) · Blood Reviews · doi:10.1016/j.blre.2012.11.001 · Cited by 101 · see citing works
When the good go bad: Mutant NPM1 in acute myeloid leukemia
Kunchala, P., Kuravi, S., Jensen, R. A., McGuirk, J. P., & Balusu, R. (2017) · Blood Reviews · doi:10.1016/j.blre.2017.11.001 · Cited by 99 · see citing works
Central role of lactate and proton in cancer cell resistance to glucose deprivation and its clinical translation
Hu, X., Chao, M., & Wu, H. (2017) · Signal Transduction and Targeted Therapy · doi:10.1038/sigtrans.2016.47 · Cited by 96 · see citing works
Consumption of NADPH for 2-HG Synthesis Increases Pentose Phosphate Pathway Flux and Sensitizes Cells to Oxidative Stress
Gelman, S. J., Naser, F. J., Mahieu, N. G., McKenzie, L. D., Dunn, G. P., Chheda, M. G., & Patti, G. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.050 · Cited by 95 · see citing works
Screen for IDH1, IDH2, IDH3, D2HGDH and L2HGDH Mutations in Glioblastoma
Krell, D., Assoku, M., Galloway, M., Mulholland, P. J., Tomlinson, I. P. M., & Bardella, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019868 · Cited by 94 · see citing works
Mutations in Epigenetic Modifiers in Myeloid Malignancies and the Prospect of Novel Epigenetic-Targeted Therapy
Fathi, A. T., & Abdel-Wahab, O. I. (2011) · Advances in Hematology · doi:10.1155/2012/469592 · Cited by 93 · see citing works
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Wrzeszczyński, K. O., Varadan, V., Byrnes, J., Lum, E., Kamalakaran, S., Levine, D. A., Dimitrova, N., Zhang, M. Q., & Lucito, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028503 · Cited by 88 · see citing works
Wild-type isocitrate dehydrogenase under the spotlight in glioblastoma
Alzial, G., Renoult, O., Paris, F., Gratas, C., Clavreul, A., & Pecqueur, C. (2021) · Oncogene · doi:10.1038/s41388-021-02056-1 · Cited by 91 · see citing works
Cancer-associated Isocitrate Dehydrogenase 1 (IDH1) R132H Mutation and d-2-Hydroxyglutarate Stimulate Glutamine Metabolism under Hypoxia
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Self-citation
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Drabovich, A. P., Pavlou, M. P., Dimitromanolakis, A., & Diamandis, E. P. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015214 · Cited by 88 · see citing works
The Role of Inflammation in Brain Cancer
Sowers, J. L., Johnson, K. M., Conrad, C. C., Patterson, J. T., & Sowers, L. C. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-0348-0837-8_4 · Cited by 90 · see citing works
Chemical, Target, and Bioactive Properties of Allosteric Modulation
van Westen, G. J. P., Gaulton, A., & Overington, J. P. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003559 · Cited by 88 · see citing works
Non-glucose metabolism in cancer cells—is it all in the fat?
Biswas, S., Lunec, J., & Bartlett, K. (2012) · Cancer and Metastasis Reviews · doi:10.1007/s10555-012-9384-6 · Cited by 86 · see citing works
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Xu, X., Gnanaprakasam, J. R., Sherman, J. W., & Wang, R. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00322 · Cited by 81 · see citing works
Molecular Diagnostics of Gliomas
Nikiforova, M. N., & Hamilton, R. L. (2011) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2010-0649-rair.1 · Cited by 82 · see citing works
BRCA1 Induces Major Energetic Metabolism Reprogramming in Breast Cancer Cells
Privat, M., Radosevic‐Robin, N., Aubel, C., Cayre, A., Penault-Llorca, F. M., Marceau, G., Sapin, V., Bignon, Y., & Morvan, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102438 · Cited by 82 · see citing works
Brain Energy Deficit as a Source of Oxidative Stress in Migraine: A Molecular Basis for Migraine Susceptibility
Borkum, J. M. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03335-9 · Cited by 80 · see citing works
Olutasidenib (FT-2102) in patients with relapsed or refractory IDH1 -mutant glioma: A multicenter, open-label, phase Ib/II trial
de la Fuente, M. I., Colman, H., Rosenthal, M. A., Tine, B. A. V., Levacic, D., Walbert, T., Gan, H. K., Vieito, M., Milhem, M. M., Lipford, K., et al. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac139 · Cited by 82 · see citing works
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Tossetta, G., & Marzioni, D. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175503 · Cited by 78 · see citing works
A Review of Radiomics and Deep Predictive Modeling in Glioma Characterization
Gore, S. A., Chougule, T., Jagtap, J., Saini, J. S., & Ingalhalikar, M. (2020) · Academic Radiology · doi:10.1016/j.acra.2020.06.016 · Cited by 76 · see citing works
Isocitrate Dehydrogenase 1 (IDH1) Mutation in Breast Adenocarcinoma Is Associated With Elevated Levels of Serum and Urine 2-Hydroxyglutarate
Fathi, A. T., Sadrzadeh, H., Comander, A. H., Higgins, M. J., Bardia, A., Perry, A. M., Burke, M. E., Silver, R. M., Matulis, C. R., Straley, K. S., et al. (2014) · The Oncologist · doi:10.1634/theoncologist.2013-0417 · Cited by 76 · see citing works
IDH1/2 mutation is a prognostic marker for survival and predicts response to chemotherapy for grade II gliomas concomitantly treated with radiation therapy
Okita, Y., Narita, Y., Miyakita, Y., Ohno, M., Matsushita, Y., Fukushima, S., Sumi, M., Ichimura, K., Kayama, T., & Shibui, S. (2012) · International Journal of Oncology · doi:10.3892/ijo.2012.1564 · Cited by 75 · see citing works
Isocitrate dehydrogenase mutations in leukemia
McKenney, A. S., & Levine, R. L. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67266 · Cited by 73 · see citing works

Intra- and extramitochondrial isocitrate dehydrogenases
Lowenstein, J. M., & Smith, S. R. (1962) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(62)90587-5 · Cited by 67 · see citing works
Enzymes Running in Reverse: Catalytic Studies on Isocitrate Dehydrogenase Mutations Implicated in Cancer
Sohl, C. D., Matteo, D. A., Grunseth, A. J., Anselmo, S. L., Gonzalez, E. R., & Kennedy, M. A. (2016) · The FASEB Journal · doi:10.1096/fasebj.30.1_supplement.1099.15
How Metabolism Informs Cancer Drug Discovery
Biller, S. A. (2012) · The FASEB Journal · doi:10.1096/fasebj.26.1_supplement.356.1
The common feature of cancer-associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting α-ketoglutarate to the oncometabolite 2-hydroxyglutarate
Ward, P. S. (2013) · Scholarly Commons (University of Pennsylvania)
Isocitrate dehydrogenase variants in cancer — Cellular consequences and therapeutic opportunities
Liu, S., Cadoux-Hudson, T. A. D., & Schofield, C. J. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.06.012 · Cited by 70 · see citing works

Authors: Reitman, Z. J., & Yan, H.
Affiliations: Duke University (US)
ORCID: Reitman, Z. J.
Yan, H.
Venue: JNCI Journal of the National Cancer Institute
Publisher: Oxford University Press (OUP)
Published: 2010-05-31
Volume: 102
Issue: 13
Pages: 932-941
ISSN: 0027-8874 (ISSN-L)
1460-2105
DOI: 10.1093/jnci/djq187
PMC: PMC2897878
OpenAlex: W2124951199
Cited by: 562
References: 88
Citations by year: 2026: 22 · 2025: 41 · 2024: 20 · 2023: 33 · 2022: 31 · 2021: 44 · 2020: 40 · 2019: 43 · 2018: 40 · 2017: 36 · 2016: 31 · 2015: 34 · 2014: 28 · 2013: 34 · 2012: 38
FWCI: 3.18
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: JNCI Journal of the National Cancer Institute (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Funders: National Cancer Institute (R01CA118822, R01CA140316)
National Institute of General Medical Sciences (T32GM007171)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Health Sciences › Medicine › Genetics › Glioma Diagnosis and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
Keywords: IDH1, IDH2, IDH1 mutation, IDH2 mutation, cancer metabolism, glioma, acute myeloid leukemia, D-2-hydroxyglutarate, oxidative stress, lipogenesis, oxygen sensing, anticancer agents
MeSH terms: Animals, Hypoxia, Arginine, Brain Neoplasms, Codon, Glioblastoma, Glucose, Glutarates, Humans, Isocitrate Dehydrogenase, Mutation, NADP, Neoplasms, Oligodendroglioma, Oncogenes, Signal Transduction, Up-Regulation, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Neoplastic, Genes, Tumor Suppressor

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Isocitrate dehydrogenase 1 and 2 mutations in cancer: alterations at a crossroads of cellular metabolism

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