Hypoxia-related Transcription factor ChIP-Seq data in T47D breast cancer cells
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ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE59935 | GEO | 2014/07/31
SECONDARY ACCESSION(S): PRJNA257093
REPOSITORIES: GEO
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Project description:We report the comprehensive genome-wide binding peaks for key factors inovled in oxygen sensing pathways, such as HIF1α, HIF1β and EglN2. In addition, we also report the genome-wide binding peaks for NRF1 in breast cancer cells We conducted HA-EglN2, HIF1α, HIF1β (ARNT) or NRF1 ChIP-Seq in the T47D cell line that overexpresses HA-EglN2 in the presence of hypoxia (1%) and DMOG treatment. T47D parental cells treated with the same condition followed by HA ChIP-seq served as the control to filter non-specific binding.
2014-07-31 | E-GEOD-59935 | biostudies-arrayexpress
Project description:In order to perform integrated analysis for EglN2 ChIP-Seq and microarray to identify EglN2 direct target genes, we performed the microarray analysis for T47D breast cancer cells with either control or EglN2 siRNA followed by hypoxia+DMOG treatment
2014-07-31 | GSE59936 | GEO
Project description:In order to perform integrated analysis for EglN2 ChIP-Seq and microarray to identify EglN2 direct target genes, we performed the microarray analysis for T47D breast cancer cells with either control or EglN2 siRNA followed by hypoxia+DMOG treatment T47D cells were transfected with either control or EglN2 siRNA in duplicate with RNAi max. 36 hours following transfection, cells were treated with hypoxia (1%) and DMOG (1 mM) for 16 hours. Following treatment, total RNA was extracted using Rnaeasy kit from Qiagen.
2014-07-31 | E-GEOD-59936 | biostudies-arrayexpress
Project description:mRNA expression was assayed from T47D SCR and T47D EGLN2 conditional knock down cell lines in order to profile the gene expression pattern regulated by EGLN2.
2009-09-19 | GSE18171 | GEO
Project description:To evaluate the role of HIF1α in modulating the m6A abundance, we conducted m6A sequencing in the Kasumi-1 cell line treated with CoCl2 and echinomycin. CoCl2 can mediate the stabilization of HIF1α protein. Echinomycin is a small-molecule inhibitor of HIF1α, which functions through sequence-specific binding to HRE to competitively inhibit HIF1α binding to its target genes. The m6A sequencing results of the Kasumi-1 cell line treated with CoCl2 and non-treated control were uploaded previously (GSE168778). The differential m6A peaks analysis between CoCl2 + echinomycin group and CoCl2 group was performed.
2022-07-01 | GSE200605 | GEO
Project description:We report the generation of CRISPR/Cas9-engineered MCF7 human breast cancer cells that lack functional HIF1α. We show that the HIF1α-dependent transcriptional response to hypoxia is severely impaired in HIF1α-mutant MCF7 cells.
2024-03-11 | GSE122059 | GEO
Project description:Histone posttranslational modifications (PTMs) are important for regulating various DNA-templated processes. Emerging evidence suggests a critical involvement of the previously less-explored histone PTMs in gene activity regulation. Here, we report the existence of a new histone PTM in the mammalian cells, hydroxylation of H3 proline 16 (H3P16-OH) catalyzed by EglN2, a proline hydroxylase. We show that EglN2-mediated H3P16-OH enhances direct binding of Lysine-Specific Demethylase 5A (KDM5A) with its substrate, H3 lysine 4 trimethylation (H3K4me3), resulting in enhanced chromatin recruitment of KDM5A and decrease of H3K4me3 at target genes. Genome-wide mapping by CUT&RUN in multiple mammalian cell models reveals a functional connection between EglN2, H3P16-OH, KDM5A and H3K4me3. Integrated analysis with RNA-Seq also identifies distinct subsets of genes that are regulated through H3P16-OH in different cell lines. This study therefore demonstrates a new player of the “histone code” by revealing a role of H3P16-OH in regulating gene expression in mammalian cells.
2022-08-02 | GSE179112 | GEO
Project description:Histone posttranslational modifications (PTMs) are important for regulating various DNA-templated processes. Emerging evidence suggests a critical involvement of the previously less-explored histone PTMs in gene activity regulation. Here, we report the existence of a new histone PTM in the mammalian cells, hydroxylation of H3 proline 16 (H3P16-OH) catalyzed by EglN2, a proline hydroxylase. We show that EglN2-mediated H3P16-OH enhances direct binding of Lysine-Specific Demethylase 5A (KDM5A) with its substrate, H3 lysine 4 trimethylation (H3K4me3), resulting in enhanced chromatin recruitment of KDM5A and decrease of H3K4me3 at target genes. Genome-wide mapping by CUT&RUN in multiple mammalian cell models reveals a functional connection between EglN2, H3P16-OH, KDM5A and H3K4me3. Integrated analysis with RNA-Seq also identifies distinct subsets of genes that are regulated through H3P16-OH in different cell lines. This study therefore demonstrates a new player of the “histone code” by revealing a role of H3P16-OH in regulating gene expression in mammalian cells.
2022-08-02 | GSE179108 | GEO
Project description:Background: Intestine epithelial hypoxia-inducible factor-1α (HIF-1α) plays a critical role in maintaining gut barrier function. The aim of this study was to determine genetic activation of intestinal HIF-1α ameliorates western diet-induced metabolic dysfunction–associated steatotic liver disease (MASLD). Methods: Male and/or female intestinal epithelial-specific Hif1α overexpression mice (Hif1α LSL/LSL;VilERcre) and wild-type littermates (Hif1α LSL/LSL) were fed with regular chow diet, high fructose (HFr) or high-fat (60% Kcal) high-fructose diet (HFHFr) for 8 weeks. Metabolic phenotypes were profiled. Results: Male Hif1α LSL/LSL;VilERcre mice exhibited markedly improved glucose tolerance compared to Hif1α LSL/LSL mice in response to HFr diet. Eight weeks HFHFr feeding led to obesity in both Hif1α LSL/LSL;VilERcre and Hif1α LSL/LSL mice. However, male Hif1α LSL/LSL;VilERcre mice exhibited markedly attenuated hepatic steatosis along with reduced liver size and liver weight compared to male Hif1α LSL/LSL mice. Moreover, HFHFr-induced systemic inflammatory responses were mitigated in male Hif1α LSL/LSL;VilERcre mice compared to male Hif1α LSL/LSL mice and those responses were not evident in female mice. Ileum RNA-seq analysis revealed that glycolysis/gluconeogenesis was up in male Hif1α LSL/LSL;VilERcre mice accompanied by increased epithelial cell proliferation. Conclusion: Our data provide evidence that genetic activation of intestinal HIF-1α markedly ameliorates western diet-induced MASLD in a sex-dependent manner. The underlying mechanism is likely attributed to HIF-1α activation induced upregulation of glycolysis, which, in turn, leading to enhanced epithelial cell proliferation and augmented gut barrier function.
2024-10-26 | GSE280362 | GEO
Project description:Background: During eye lens development the fetal vasculature regresses leaving the lens without a direct oxygen source. Both embryonically and throughout adult life, the lens contains a decreasing oxygen gradient from the surface to the core that parallels the natural differentiation of immature surface epithelial cells into mature core transparent fiber cells. These properties of the lens suggest a potential role for hypoxia in the regulation of genes required for mature lens structure and function. Since HIF1α is a master regulator of the hypoxic response, these lens properties also implicate HIF1α as a potential requirement for lens formation and homeostasis. Here, we employed a multiomics approach combining CUT&RUN, RNAseq and ATACseq analysis to establish the genomic complement of lens HIF1α binding sites, genes activated or repressed by HIF1α and the chromatin states of HIF1α-regulated genes. Results: CUT&RUN analysis revealed 8,375 HIF1α-DNA binding complexes in the chick lens genome. 1,190 HIF1α-DNA binding complexes were significantly clustered within chromatin accessible regions (χ2 test p < 1x10-55) identified by ATACseq. Formation of the identified HIF1α-DNA complexes paralleled the activation or repression of 526 genes, 116 of which contained HIF1α binding sites within 10kB of the transcription start sites. Some of the identified HIF1α genes have previously established lens functions while others have novel functions never before examined in the lens. GO and pathway analysis of these genes implicate HIF1α in the control of a wide-variety of cellular pathways potentially critical for lens formation, structure and function including glycolysis, cell cycle regulation, chromatin remodeling, Notch and Wnt signaling, differentiation, development, and transparency. Conclusions: These data establish the first functional map of genomic HIF1α-DNA complexes in the eye lens. They identify HIF1α as an important regulator of a wide-variety of genes previously shown to be critical for lens formation and function and they reveal a requirement for HIF1α in the regulation of a wide-variety of genes not yet examined for lens function. They support a requirement for HIF1α in lens development, structure and function and they provide a basis for understanding the potential roles and requirements for HIF1α in the development, structure and function of more complex tissues.
2021-07-07 | GSE166632 | GEO