UNASSIGNED: The onset and progression of @entity0 are linked to genetic and epigenetic changes that alter the normal programming of cells. Epigenetic modifications of DNA and histones contribute to chromatin structure that result in the activation or repression of gene expression. Several epigenetic pathways have been shown to be highly deregulated in @entity5 cells. Targeting specific histone modifications represents a viable strategy to prevent oncogenic transformation, @entity5 growth or @entity3 . Methylation of histone H3 @entity376 4 has been extensively studied and shown to mark genes for expression; however this residue can also be acetylated and the specific function of this alteration is less well known. To define the relative roles of histone H3 methylation (H3K4me3) and acetylation (H3K4ac) in @entity0 , we determined genomic regions enriched for both marks in normal-like (MCF10A), transformed (MCF7) and metastatic (MDA-MB-231) cells using a genome-wide ChIP-Seq approach. Our data revealed a genome-wide gain of H3K4ac associated with both early and late @entity0 cell phenotypes, while gain of H3K4me3 was predominantly associated with late stage @entity5 cells. Enrichment of H3K4ac was over-represented at promoters of genes associated with @entity5 -related phenotypic traits, such as @entity172 response and epithelial-to-mesenchymal transition pathways. Our findings highlight an important role for H3K4ac in predicting epigenetic changes associated with early stages of transformation. In addition, our data provide a valuable resource for understanding epigenetic signatures that correlate with known @entity0 -associated oncogenic pathways.

Histone H3 XXXX 4 acetylation and methylation dynamics define @entity0 subtypes.

@entity172 :: ('MESH:D004967', 'Chemical') :: ['estrogen'] @entity0 :: ('MESH:D001943', 'Disease') :: ['breast cancer'] @entity5 :: ('MESH:D009369', 'Disease') :: ['tumor', 'cancer'] @entity376 :: ('CHEBI:25094', 'Chemical') :: ['lysine'] @entity3 :: ('MESH:D009362', 'Disease') :: ['metastasis']
@entity376 :: (CHEBI:25094,Chemical) :: ['lysine']
