作者
Dan Rohle,Janeta Popovici-Müller,Nicolaos Palaskas,Şevin Turcan,Christian Grommes,Carl Campos,Jennifer Tsoi,Owen Clark,Barbara Oldrini,Evangelia Komisopoulou,Kaiko Kunii,Alicia Pedraza,Stefanie Schalm,Lee Silverman,Alexandra Miller,Fang Wang,Hua Yang,Yue Chen,Andrew Kernytsky,Marc K. Rosenblum,Wei Liu,Scott A. Biller,Shinsan M. Su,Cameron Brennan,Timothy A. Chan,Thomas G. Graeber,Katharine Yen,Ingo K. Mellinghoff
摘要
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 (mIDH1) to produce R-2-hydroxyglutarate (R-2HG). Under conditions of near-complete R-2HG inhibition, the mIDH1 inhibitor induced demethylation of histone H3K9me3 and expression of genes associated with gliogenic differentiation. Blockade of mIDH1 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 mIDH1 may promote glioma growth through mechanisms beyond its well-characterized epigenetic effects.