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Isocitrate dehydrogenase gene variants in cancer and their clinical significance.
Cadoux-Hudson, Thomas; Schofield, Christopher J; McCullagh, James S O.
Afiliación
  • Cadoux-Hudson T; Chemistry Research Laboratory, Department of Chemistry and the Ineos Institute for Antimicrobial Research, University of Oxford, Mansfield Road, Oxford OX1 3TA, U.K.
  • Schofield CJ; Chemistry Research Laboratory, Department of Chemistry and the Ineos Institute for Antimicrobial Research, University of Oxford, Mansfield Road, Oxford OX1 3TA, U.K.
  • McCullagh JSO; Chemistry Research Laboratory, Department of Chemistry and the Ineos Institute for Antimicrobial Research, University of Oxford, Mansfield Road, Oxford OX1 3TA, U.K.
Biochem Soc Trans ; 49(6): 2561-2572, 2021 12 17.
Article en En | MEDLINE | ID: mdl-34854890
Human isocitrate dehydrogenase (IDH) genes encode for the IDH1, 2 & 3 isoenzymes which catalyse the formation of 2-oxoglutarate from isocitrate and are essential for normal mammalian metabolism. Although mutations in these genes in cancer were long thought to lead to a 'loss of function', combined genomic and metabolomic studies led to the discovery that a common IDH 1 mutation, present in low-grade glioma and acute myeloid leukaemia (AML), yields a variant (R132H) with a striking change of function leading to the production of (2R)-hydroxyglutarate (2HG) which consequently accumulates in large quantities both within and outside cells. Elevated 2HG is proposed to promote tumorigenesis, although the precise mechanism by which it does this remains uncertain. Inhibitors of R132H IDH1, and other subsequently identified cancer-linked 2HG producing IDH variants, are approved for clinical use in the treatment of chemotherapy-resistant AML, though resistance enabled by additional substitutions has emerged. In this review, we provide a current overview of cancer linked IDH mutations focussing on their distribution in different cancer types, the effects of substitution mutations on enzyme activity, the mode of action of recently developed inhibitors, and their relationship with emerging resistance-mediating double mutations.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Isocitrato Deshidrogenasa / Isoenzimas / Neoplasias Límite: Humans Idioma: En Revista: Biochem Soc Trans Año: 2021 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Isocitrato Deshidrogenasa / Isoenzimas / Neoplasias Límite: Humans Idioma: En Revista: Biochem Soc Trans Año: 2021 Tipo del documento: Article Pais de publicación: Reino Unido