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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Bivalency - Histone H3 Lysine4 and Histone H3 Lysine27 Methylation Dynamics

ABSTRACT: The molecular signature at histone H3K4me3 and H3K27me3 involved in epigenetic regulation of normal (MCF10A) and transformed (MCF7, MDA-MB-231) breast cells using ChIP-Seq technology. This study examines the dynamic distribution of H3K4me3, associated with active chromatin, and H3K27me3, associated with repressed chromatin, histone modifications to provide an understanding of the changes in epigenetic regulation associated with the unique breast cancer subtypes. histone H3K4me3 and H3K27me3 ChIP-seq normal (MCF10A) and transformed (MCF7, MDA-MB-231) breast cells Please note that the 'H3K4me3' and 'input' data are duplicated records of the samples represented in GSE69377 for the convenient retrieval of the complete raw data from SRA.

ORGANISM(S): Homo sapiens

SUBMITTER: Joe Boyd

PROVIDER: E-GEOD-77772 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Oncofetal Epigenetic Bivalency in Breast Cancer Cells: H3K4 and H3K27 Tri-Methylation as a Biomarker for Phenotypic Plasticity.

Messier Terri L TL Boyd Joseph R JR Gordon Jonathan A R JA Stein Janet L JL Lian Jane B JB Stein Gary S GS

Journal of cellular physiology 20160310 11

Alterations in the epigenetic landscape are fundamental drivers of aberrant gene expression that contribute to cancer progression and pathology. Understanding specific modes of epigenetic regulation can be used to identify novel biomarkers or targets for therapeutic intervention to clinically treat solid tumors and leukemias. The bivalent marking of gene promoters by H3K4me3 and H3K27me3 is a primary mechanism to poise genes for expression in pluripotent embryonic stem cells (ESC). In this study ...[more]

PMID: 26916849

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Histone H3 Lysine4 Acetylation-Methylation Dynamics Define Breast Cancer Subtypes [ChIP-seq]

Project description:The molecular signature at histone H3K4 involved in epigenetic regulation of normal (MCF10A) and transformed (MCF7, MDA-MB-231) breast cells using ChIP-Seq technology. This study examines the dynamic distribution of H3K4me3 and H3K4ac histone modification associated with active chromatin to provide an understanding of the changes in epigenetic regulation associated with the unique breast cancer subtypes. H3K4me3 and H3K4ac histone modification study in normal (MCF10A) and transformed (MCF7, MDA-MB-231) breast cells using ChIP-Seq technology

2016-02-10 | E-GEOD-69377 | biostudies-arrayexpress

Histone H3 lysine 4 acetylation-methylation dynamics define breast cancer subtypes [RNA-seq]

Project description:The onset and progression of breast cancer 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 results in the activation or repression of gene expression. Several epigenetic pathways have been shown to be highly deregulated in cancer cells. Targeting specific histone modifications represents a viable strategy to prevent oncogenic transformation, tumor growth or metastasis. Methylation of histone H3 lysine 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 breast cancer, 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 breast cancer cell phenotypes, while gain of H3K4me3 was predominantly associated with late stage cancer cells. Enrichment of H3K4ac was overrepresented at promoters of genes associated with cancer-related phenotypic traits, such as estrogen 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 breast cancer-associated oncogenic pathways. RNA-Seq of cell lines MCF10A, MCF7 and MDA-MB-231.

2016-02-10 | E-GEOD-75168 | biostudies-arrayexpress

Bivalency - Histone H3 Lysine4 and Histone H3 Lysine27 Methylation Dynamics

Project description:The molecular signature at histone H3K4me3 and H3K27me3 involved in epigenetic regulation of normal (MCF10A) and transformed (MCF7, MDA-MB-231) breast cells using ChIP-Seq technology. This study examines the dynamic distribution of H3K4me3, associated with active chromatin, and H3K27me3, associated with repressed chromatin, histone modifications to provide an understanding of the changes in epigenetic regulation associated with the unique breast cancer subtypes.

2016-03-24 | GSE77772 | GEO

Histone H3 Lysine4 Acetylation-Methylation Dynamics Define Breast Cancer Subtypes [ChIP-seq]

2016-02-10 | GSE69377 | GEO

Differential Gene Expression between MCF10A and MCF7 cells

Project description:These RNA-seq data were generated to correlate with genomic interaction data in a related Hi-C analysis. MCF10A is a normal-like mammary epithelial cell line and MCF7 is a transformed estrogen responsive breast cancer cell line derived from a metastatic site; both are commonly used in models of breast cancer progression. Analysis revealed a set of genes related to repression of WNT signalling that were both up-regulated in MCF7 and located in genomic regions that had transitioned from closed to open structure in MCF7. RNA-seq of MCF10A and MCF7 cells. 3 replicates each. Sequencing was strand-specific and conducted on ribo-depleted RNA.

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Histone H3 lysine 4 acetylation-methylation dynamics define breast cancer subtypes [RNA-seq]

2016-02-10 | GSE75168 | GEO

PARP-1, H3 and H3K4me3 ChIP-chip from MCF7 cells

Project description:We are examining the mechanisms by which the nuclear enzyme PARP-1 regulates gene expression. We performed ChIP-chip for PARP-1, histone H3 and H3K4me3 (lysine 4 trimethylation on histone H3) in MCF7 breast carcinoma cells, and looked at 23550 RefSeq genes to determine binding patterns of these factors at promoters. Each experiment was performed in duplicate. ChIP-chip biological replicates for PARP-1, H3 and H3K4me3 (2 replicates each) from MCF7 human breast carcinoma cells are included.

2010-09-20 | E-GEOD-19619 | biostudies-arrayexpress

Phosphoproteomic analysis of breast cancer-derived extracellular vesicles reveals disease-specific phosphorylated enzymes

Project description:Small membrane-derived extracellular vesicles have been proposed to participate in several cancer diseases, including breast cancer. We performed phosphoproteomic analysis of breast cancer-derived small extracellular vesicles (sEVs) to provide insight into the molecular and cellular regulatory mechanisms important for breast cancer tumor progression and metastasis. We examined 3 cell lines as models for breast cancer: MCF10A (non-metastatic), MCF7 (estrogen and progesterone receptor positive, metastatic) and MDA-MB-231 (triple-negative, highly metastatic). To obtain a comprehensive overview of the sEV phosphoproteme derived from each cell line, an effective enrichment phosphopeptide techniques with IMAC and TiO2, followed by LC-MS/MS was achieved. In total, 2003 phosphopeptides on which 207, 854 and 1335 have been identified in MCF10A, MCF7 and MDA-MB-231cell lines, respectively. These phosphorylation sites were mapped to 855 distinct proteins, covering a wide range of functions. These proteins are associated with larger number of diseases and the most common diseases are related to cancer. Among the phosphoproteins identified, we validated four enzymes associated to cancer and present only in sEVs isolated from MCF7 and MDA-MB-231 cell lines: ATP citrate lyase (ACLY), phosphofructokinase-M (PFKM), Sirtuin-1 (SIRT1) and Sirtuin-6 (SIRT6). With the exception of PFKM, the specific activity of these enzymes was significantly higher in MDA-MB-231 when compared with MCF10A-derived sEVs. This study demonstrates that sEVs contain functional metabolic enzymes that could be further explored for their potential in early BC diagnostic and therapeutic applications.

2022-02-28 | PXD030424 | Pride

tsRNA microarray of parental normal-like and breast cancer cell lines and with inhibited or induced RUNX1 expression

Project description:The expression levels of tRNA-derived small RNA, known as tsRNA, were interrogated in the following parental cell lines: MCF10A normal-like mammary epithelial cell, MCF7, MCF10AT1, MCF10CA1a, and MDA-MB-231 breast cancer cells. In addition, tsRNA expression was determined after shRNA-inhibition of RUNX1 in MCF10A cells or RUNX1 induction in MCF10CA1a cells.

2020-01-01 | GSE142382 | GEO

Lysine acetolome of breast cancer-derived small extracellular vesicles reveals specific acetylation pattern for metabolic enzymes

Project description:Cancer-derived small extracellular vesicles have been proposed as promising potential biomarkers for diagnosis and prognosis of breast cancer (BC). We performed a proteomic study of lysine acetylation of breast cancer-derived small extracellular vesicles (sEVs) to understand the potential role of the aberrant acetylated proteins in the metastasis and progression of BC. Three cell lines were used as models for this study: MCF10A (non-metastatic), MCF7 (estrogen and progesterone receptor positive, metastatic) and MDA-MB-231 (triple-negative, highly metastatic). For a com-prehensive protein acetylation analysis of the sEVs derived from each cell line, acetylated peptides were enriched using the anti-acetyl-lysine antibody, followed by LC-MS/MS analysis. In total, 118 lysine acetylated peptides of which 22, 58 and 82 have been identified in MCF10A, MCF7 and MDA-MB-231 cell lines, respectively. These acetylated peptides were mapped to 60 distinct pro-teins and mainly identified proteins involved in metabolic pathways. Among those identified acetylated proteins presented in cancer-derived sEVs (MCF7, MDA-MB-231) are proteins associ-ated with glycolysis pathway, annexins and histones. Five enzymes from the glycolytic pathway, present only in sEVs isolated from cancer-derived sEVs cell lines, were validated. These include aldolase (ALDOA), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), phosphoglycerate kinase (PGK 1), enolase (ENO) and pyruvate kinase M1/2 (PKM). For three of these enzymes, ALDOA, PGK 1 and ENO, the specific enzymatic activity was significantly higher in MDA-MB-231 when compared with MCF10A-derived sEVs. This study reveals that sEVs contain acetylated glycolytic metabolic enzymes that could be interesting potential candidates for early BC diagnostics.

2023-07-20 | PXD040413 | Pride

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