Characterizing an HSF1-dependent transcriptional program in metastatic lung adenocarcinoma
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ABSTRACT:
PROVIDER: PRJNA627725 | ENA |
REPOSITORIES: ENA
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Project description:The purpose of this study was to identify gene targets differentially regulated by shRNA-mediated knockdown of the HSF1 transcription factor in the brain-metastatic lung adenocarcinoma cell line PC9-BrM3.
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Project description:This SuperSeries is composed of the following subset Series: GSE38232: HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers [gene expression] GSE38901: HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers [ChIP-Seq] Refer to individual Series
2012-08-06 | E-GEOD-38912 | biostudies-arrayexpress
Project description:Heat-Shock Factor 1 (HSF1), master regulator of the heat-shock response, facilitates malignant transformation, cancer cell survival and proliferation in model systems. The common assumption is that these effects are mediated through regulation of heat-shock protein (HSP) expression. However, the transcriptional network that HSF1 coordinates directly in malignancy and its relationship to the heat-shock response have never been defined. By comparing cells with high and low malignant potential alongside their non-transformed counterparts, we identify an HSF1-regulated transcriptional program specific to highly malignant cells and distinct from heat shock. Cancer-specific genes in this program support oncogenic processes: cell-cycle regulation, signaling, metabolism, adhesion and translation. HSP genes are integral to this program, however, even these genes are uniquely regulated in malignancy. This HSF1 cancer program is active in breast, colon and lung tumors isolated directly from human patients and is strongly associated with metastasis and death. Thus, HSF1 rewires the transcriptome in tumorigenesis, with prognostic and therapeutic implications. ChIP-seq was used to characterize HSF1 binding
2012-08-07 | E-GEOD-38901 | biostudies-arrayexpress
Project description:Heat shock factor 1 (HSF1) is well known for its role in the heat shock response (HSR), where it drives a transcriptional program comprising heat shock protein (HSP) genes, and in tumorigenesis, where it drives a program comprising HSPs and many non-canonical target genes that support malignancy. Here, we find that HSF2, an HSF1 paralog with no significant role in the HSR, physically and functionally interacts with HSF1 across diverse types of cancer. HSF1 and HSF2 have strikingly similar chromatin occupancy and regulate a common set of genes which include both HSPs and non-canonical transcriptional targets with roles critical in supporting malignancy. Loss of either HSF1 or HSF2 results in a dysregulated response to nutrient stresses in vitro and reduced tumor progression in cancer cell line xenografts. Taken together, these findings establish HSF2 as a critical cofactor of HSF1 in driving a cancer cell transcriptional program to support the anabolic malignant state.
2022-03-15 | GSE194098 | GEO
Project description:Heat-Shock Factor 1 (HSF1), master regulator of the heat-shock response, facilitates malignant transformation, cancer cell survival and proliferation in model systems. The common assumption is that these effects are mediated through regulation of heat-shock protein (HSP) expression. However, the transcriptional network that HSF1 coordinates directly in malignancy and its relationship to the heat-shock response have never been defined. By comparing cells with high and low malignant potential alongside their non-transformed counterparts, we identify an HSF1-regulated transcriptional program specific to highly malignant cells and distinct from heat shock. Cancer-specific genes in this program support oncogenic processes: cell-cycle regulation, signaling, metabolism, adhesion and translation. HSP genes are integral to this program, however, even these genes are uniquely regulated in malignancy. This HSF1 cancer program is active in breast, colon and lung tumors isolated directly from human patients and is strongly associated with metastasis and death. Thus, HSF1 rewires the transcriptome in tumorigenesis, with prognostic and therapeutic implications. We used microarrays to examine affect of HSF1 depletion on gene expression in cancer cell lines. Three cancer cell lines (BPLER, HMLER & MCF7) were transduced with either control shRNAi (Scramble or GFP) or an shRNAi that targets and depletes HSF1 (hA6). Another BPLER sample was subjected to a 1H, 42M-KM-^Z C heat shock. Two biological replicates for all samples.
2012-08-06 | E-GEOD-38232 | biostudies-arrayexpress
Project description:Heat-Shock Factor 1 (HSF1), master regulator of the heat-shock response, facilitates malignant transformation, cancer cell survival and proliferation in model systems. The common assumption is that these effects are mediated through regulation of heat-shock protein (HSP) expression. However, the transcriptional network that HSF1 coordinates directly in malignancy and its relationship to the heat-shock response have never been defined. By comparing cells with high and low malignant potential alongside their non-transformed counterparts, we identify an HSF1-regulated transcriptional program specific to highly malignant cells and distinct from heat shock. Cancer-specific genes in this program support oncogenic processes: cell-cycle regulation, signaling, metabolism, adhesion and translation. HSP genes are integral to this program, however, even these genes are uniquely regulated in malignancy. This HSF1 cancer program is active in breast, colon and lung tumors isolated directly from human patients and is strongly associated with metastasis and death. Thus, HSF1 rewires the transcriptome in tumorigenesis, with prognostic and therapeutic implications.
2012-08-07 | GSE38232 | GEO
Project description:Heat-Shock Factor 1 (HSF1), master regulator of the heat-shock response, facilitates malignant transformation, cancer cell survival and proliferation in model systems. The common assumption is that these effects are mediated through regulation of heat-shock protein (HSP) expression. However, the transcriptional network that HSF1 coordinates directly in malignancy and its relationship to the heat-shock response have never been defined. By comparing cells with high and low malignant potential alongside their non-transformed counterparts, we identify an HSF1-regulated transcriptional program specific to highly malignant cells and distinct from heat shock. Cancer-specific genes in this program support oncogenic processes: cell-cycle regulation, signaling, metabolism, adhesion and translation. HSP genes are integral to this program, however, even these genes are uniquely regulated in malignancy. This HSF1 cancer program is active in breast, colon and lung tumors isolated directly from human patients and is strongly associated with metastasis and death. Thus, HSF1 rewires the transcriptome in tumorigenesis, with prognostic and therapeutic implications.
2012-08-07 | GSE38901 | GEO
Project description:Upon heat shock, Hsf1 protein is extensively phosphorylated, however, this modification is inhibited by an hsf1-bal mutation. To get genome-wide effect of the hyperphosphorylation on Hsf1-regulated transcription, the heat-induced gene expression profiles in HSF1 and hsf1-bal cells were compared. Keywords: stress response
2005-09-27 | GSE3361 | GEO
Project description:The heat shock response is an ancient and ubiquitous program allowing organisms to survive adverse environmental conditions. In S. cerevisiae, three transcription factors, Hsf1, Msn2 and Msn4, are thought to regulate the stress response. While Msn2/4 can be deleted, Hsf1 is essential. By combining the depletion of Hsf1 with the deletion of Msn2 and Msn4, we were able to switch off the central stress response. We show that the transcription factors Hsf1 and Msn2/4 follow different strategies and regimes: Whereas Msn2/4 are responsible for a broad metabolic response, Hsf1 triggers a direct chaperone response to stabilize and repair unfolded proteins. Exposure of cells lacking Msn2/4 and Hsf1 to thermal stress resulted in massive protein aggregation. Comparison with wildtype yeast revealed that among the proteins rescued by the stress response are many essential proteins.
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Project description:HSF1 orchestrates a transcriptional program vital for cancer cells. In this study we assayed for genome-wide localization of HSF1 enrichment in the 451Lu melanoma in untreated cells. These results revealed a transcriptional program enriched for metastasis-related genes. Twenty million cells were used for the ChIP and precipitated using 5 micrograms of antibody (cell signaling, 4356) against human HSF1
2015-02-20 | E-GEOD-63589 | biostudies-arrayexpress