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Rohle, Dan; Popovici-Muller, Janeta; Palaskas, Nicolaos; Turcan, Sevin; Grommes, Christian; Campos, Carl; Tsoi, Jennifer; Clark, Owen; Oldrini, Barbara; Komisopoulou, Evangelia; Kunii, Kaiko; Pedraza, Alicia; Schalm, Stefanie; Silverman, Lee; Miller, Alexandra; Wang, Fang; Yang, Hua; Chen, Yue; Kernytsky, Andrew; Rosenblum, Marc K.; Liu, Wei; Biller, Scott A.; Su, Shinsan M.; Brennan, Cameron W.; Chan, Timothy A.; Graeber, Thomas G.; Yen, Katharine E.; Mellinghoff, Ingo K.
Science, 05/2013, Letnik: 340, Številka: 6132Journal Article
The recent discovery of mutations in metabolic enzymes has rekindled interest in harnessing the altered metabolism of cancer cells for cancer therapy. One potential drug target is isocitrate dehydrogenase 1 (IDH1), which is mutated in multiple human cancers. Here, we examine the role of mutant IDH1 in fully transformed cells with endogenous IDH1 mutations. A selective R132H-IDH1 inhibitor (AGI-5198) identified through a high-throughput screen blocked, in a dose-dependent manner, the ability of the mutant enzyme (m1DH1) to produce R-2-hydroxyglutarate (R-2HG). Under conditions of near-complete R-2HG inhibition, the m1DH1 inhibitor induced demethylation of histone H3K9me3 and expression of genes associated with gliogenic differentiation. Blockade of m1DH1 impaired the growth of IDH1-mutant—but not IDH1-wild-type—glioma cells without appreciable changes in genome-wide DNA methylation. These data suggest that m1DH1 may promote glioma growth through mechanisms beyond its well-characterized epigenetic effects.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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Vir: Osebne bibliografije
in: SICRIS
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