Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Gene expression data of pHGG tumor samples


ABSTRACT: Pediatric high-grade gliomas (pHGGs) harboring the K27M mutation of H3F3A (histone H3.3) are characterized by global reduction of the repressive histone mark H3K27me3 and DNA hypomethylation. Analysis of K27M-induced changes on H3K27me3 occupancy and DNA methylation at differentially expresed genes (K27M vs. wild-type H3.3) in primary pHGG tumor samples. 22 glioblastoma samples from pHGG patients were selected for RNA extraction and hybridization on Affymetrix Affymetrix Human Genome U133 Plus 2.0 Arrays. Expression profiling data of 17 pHHGs are part of our previous study (GSE36245 or GSE34824).

ORGANISM(S): Homo sapiens

SUBMITTER: Marcel Kool 

PROVIDER: E-GEOD-49822 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

Reduced H3K27me3 and DNA hypomethylation are major drivers of gene expression in K27M mutant pediatric high-grade gliomas.

Bender Sebastian S   Tang Yujie Y   Lindroth Anders M AM   Hovestadt Volker V   Jones David T W DT   Kool Marcel M   Zapatka Marc M   Northcott Paul A PA   Sturm Dominik D   Wang Wei W   Radlwimmer Bernhard B   Højfeldt Jonas W JW   Truffaux Nathalène N   Castel David D   Schubert Simone S   Ryzhova Marina M   Seker-Cin Huriye H   Gronych Jan J   Johann Pascal David PD   Stark Sebastian S   Meyer Jochen J   Milde Till T   Schuhmann Martin M   Ebinger Martin M   Monoranu Camelia-Maria CM   Ponnuswami Anitha A   Chen Spenser S   Jones Chris C   Witt Olaf O   Collins V Peter VP   von Deimling Andreas A   Jabado Nada N   Puget Stephanie S   Grill Jacques J   Helin Kristian K   Korshunov Andrey A   Lichter Peter P   Monje Michelle M   Plass Christoph C   Cho Yoon-Jae YJ   Pfister Stefan M SM  

Cancer cell 20131031 5


Two recurrent mutations, K27M and G34R/V, within histone variant H3.3 were recently identified in ∼50% of pHGGs. Both mutations define clinically and biologically distinct subgroups of pHGGs. Here, we provide further insight about the dominant-negative effect of K27M mutant H3.3, leading to a global reduction of the repressive histone mark H3K27me3. We demonstrate that this is caused by aberrant recruitment of the PRC2 complex to K27M mutant H3.3 and enzymatic inhibition of the H3K27me3-establis  ...[more]

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