HCSGD entry for HSF1
1. General information
| Official gene symbol | HSF1 |
|---|---|
| Entrez ID | 3297 |
| Gene full name | heat shock transcription factor 1 |
| Other gene symbols | HSTF1 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0001162 | RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding | IDA | molecular_function |
| GO:0001892 | Embryonic placenta development | IEA | biological_process |
| GO:0003682 | Chromatin binding | IEA | molecular_function |
| GO:0003700 | Sequence-specific DNA binding transcription factor activity | IEA | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005634 | Nucleus | IDA IEA | cellular_component |
| GO:0005730 | Nucleolus | IDA | cellular_component |
| GO:0005737 | Cytoplasm | IDA IEA | cellular_component |
| GO:0006351 | Transcription, DNA-templated | IEA | biological_process |
| GO:0006468 | Protein phosphorylation | IEA | biological_process |
| GO:0006952 | Defense response | IEA | biological_process |
| GO:0007143 | Female meiosis | IEA | biological_process |
| GO:0007283 | Spermatogenesis | IEA | biological_process |
| GO:0008285 | Negative regulation of cell proliferation | IEA | biological_process |
| GO:0009408 | Response to heat | IEA | biological_process |
| GO:0032496 | Response to lipopolysaccharide | IEA | biological_process |
| GO:0032720 | Negative regulation of tumor necrosis factor production | IEA | biological_process |
| GO:0034605 | Cellular response to heat | IDA | biological_process |
| GO:0040018 | Positive regulation of multicellular organism growth | IEA | biological_process |
| GO:0043234 | Protein complex | IEA | cellular_component |
| GO:0043565 | Sequence-specific DNA binding | IEA | molecular_function |
| GO:0045120 | Pronucleus | IEA | cellular_component |
| GO:0045944 | Positive regulation of transcription from RNA polymerase II promoter | IDA | biological_process |
| GO:0060136 | Embryonic process involved in female pregnancy | IEA | biological_process |
| GO:0090231 | Regulation of spindle checkpoint | IEA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.0230808556 | 0.9735264694 | 0.3616227976 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Up | 0.1403607541 |
| GSE13712_SHEAR | Up | 0.1156120346 |
| GSE13712_STATIC | Down | -0.0923608864 |
| GSE19018 | Down | -0.0002596380 |
| GSE19899_A1 | Up | 0.1223329560 |
| GSE19899_A2 | Up | 0.4401620942 |
| PubMed_21979375_A1 | Up | 1.7942577536 |
| PubMed_21979375_A2 | Up | 0.6647102913 |
| GSE35957 | Up | 0.0603037927 |
| GSE36640 | Up | 0.1726636620 |
| GSE54402 | Up | 0.1926601327 |
| GSE9593 | Up | 0.2741420120 |
| GSE43922 | Up | 0.2566539208 |
| GSE24585 | Down | -0.1685951640 |
| GSE37065 | Down | -0.1309325488 |
| GSE28863_A1 | Up | 0.0979612250 |
| GSE28863_A2 | Up | 0.1720658089 |
| GSE28863_A3 | Up | 0.4010972158 |
| GSE28863_A4 | Up | 0.1009462075 |
| GSE48662 | Up | 0.3215145141 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-26b-5p | MIMAT0000083 | MIRT029982 | Microarray | Functional MTI (Weak) | 19088304 |
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- mirRecord
No target information from mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 14 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 25292174 | The levels of HSP70, its major transcription factor, HSF1, and JNKs were assessed by immunoblotting hepatic and visceral adipose tissue; data were confirmed by immunohistochemistry |
| 25292174 | RESULTS: In both liver and adipose tissue, decreased HSP70 levels, paralleled by similar reductions in HSF1 and reduced plasma antioxidant enzyme activities, correlated with insulin resistance and with NAFLD progression (expression levels were as follows: ST > SH > SH + F) |
| 25292174 | CONCLUSIONS: Decreased HSF1 levels in the liver and fat of obese patients correlated with impairment of HSP70 in an NAFLD stage-dependent manner |
| 25193128 | In order to understand how cells distinguish between mild and severe stress, we have investigated the extent of early and immediate HS response by analyzing the nuclear translocation of the transcription factor heat shock factor-1 (HSF1), in serially passaged normal adult human facial skin fibroblasts exposed to mild (41 degrees C) or severe (43 degrees C) HS |
| 25193128 | Cells respond differently when exposed to mild and severe HS at different passage levels in terms of the extent of HSF1 translocation |
| 25193128 | In early passage young cells there was a 5-fold difference between mild and severe HS in the extent of HSF1 translocation |
| 25193128 | However, in near senescent late passage cells, the difference between mild and severe stress in terms of the extent of HSF1 translocation was reduced to less than 2-fold |
| 25193128 | One of the reasons for this age-related attenuation of heat shock response is due to the fact there was a higher basal level of HSF1 in the nuclei of late passage cells, which is indicative of increased intrinsic stress during cellular aging |
| 24878874 | Sirtuin-1 is responsible for the induction of heat shock transcription factor-1 mRNA expression and for the stabilization of heat shock transcription factor-1 in a high-profile activity state |
| 22510478 | The heat shock transcription factor Hsf1 is downregulated in DNA damage-associated senescence, contributing to the maintenance of senescence phenotype |
| 22510478 | The HSR suppression was associated with inhibition of both activity and transcription of the heat shock transcription factor Hsf1 |
| 22510478 | Importantly, we uncovered a positive feedback regulation, where suppression of Hsf1 further activates the p38-NF-kappaB-SASP pathway, which in turn promotes senescence |
| 22510478 | Overexpression of Hsf1 inhibited the p38-NFkappaB-SASP pathway and partially relieved senescence |
| 22510478 | Therefore, downregulation of Hsf1 plays an important role in the development or in the maintenance of DNA damage signaling-induced cell senescence |
| 20622894 | Heat-shock transcription factor HSF1 has a critical role in human epidermal growth factor receptor-2-induced cellular transformation and tumorigenesis |
| 20622894 | The heat-shock transcription factor HSF1 was recently shown to have a key role in the development of tumors associated with activation of Ras or inactivation of p53 |
| 20622894 | Here, we show that HSF1 is required for the cell transformation and tumorigenesis induced by the human epidermal growth factor receptor-2 (HER2) oncogene responsible for aggressive breast tumors |
| 20622894 | However, expression of HER2 in MCF-10A cells with knockdown of HSF1 did not cause either foci formation or tumor growth in xenografts |
| 20622894 | The antitumorigenic effect of downregulation of HSF1 was associated with HER2-induced accumulation of the cyclin-dependent kinase inhibitor p21 and decrease in the mitotic regulator survivin, which resulted in growth inhibition and cell senescence |
| 20622894 | In fact, either knockout of p21 or overexpression of survivin alleviated these effects of HSF1 knockdown |
| 20622894 | The proliferation of certain human HER2-positive breast cancer lines also requires HSF1, as its knockdown led to upregulation of p21 and/or decrease in survivin, precipitating growth arrest |
| 20622894 | Therefore, HSF1 is critical for proliferation of HER2-expressing cells, most likely because it maintains the levels of HSPs, which in turn control regulators of senescence p21 and survivin |
| 19706382 | Enhancing stress responsive factors HSF-1 or DAF-16 suppresses misfolding of these metastable folding sensors and restores the ability of the cell to maintain a functional proteome |
| 19119860 | The most likely candidates for delaying senescence are the longevity-linked transcription factors DAF16 and HSF1 |
| 19119860 | If one were to engineer negligible senescence, a key target would be the heat shock protein axis regulated by HSF1 |
| 19119860 | Reduced HSF1 activity appears to accelerate tissue aging and shortens life span |
| 19119860 | Conversely, over-expression of HSF1 increases life span and decreases amyloid toxicity in animal models |
| 19097133 | To better understand the underlying mechanism, we evaluated changes in the regulation and function of the HSF1 transcription factor |
| 19097133 | We show that the activation of HSF1 both in vivo and in vitro was decreased as a function of age, and this was attributable to a change in the regulation of HSF1 as the abundance of HSF1 protein and mRNA was unaffected |
| 19097133 | HSF1 was primarily cytosolic in young cells maintained at 37 degrees C, and heat shock promoted its quantitative nuclear translocation and trimerization |
| 19097133 | In old cells, some HSF1 was nuclear sequestered at 37 degrees C, and heat shock failed to promote the quantitative trimerization of HSF1 |
| 19097133 | These changes in HSF1 could be reproduced by treating young cells with H2O2 to stunt them into premature senescence |
| 19097133 | Experiments using isoelectric focusing and Western blot showed age-dependent changes in the mobility of HSF1 in a pattern consistent with its S-glutathiolation and S-nitrosylation; these changes could be mimicked by treating young cells with H2O2 |
| 19097133 | Our results demonstrated dynamic age-dependent changes in the regulation but not the amount of HSF1 |
| 19097133 | These changes are likely mediated by oxidative events that promote reversible and irreversible modification of HSF1 including S-glutathiolation and S-nitrosylation |
| 18325704 | To determine the mechanism of REMFS-induced effects, analysis of the cellular heat shock response revealed Hsp90 release from the heat shock transcription factor (HSF1) |
| 18325704 | Furthermore, REMFS increased HSF1 phosphorylation, enhanced HSF1-DNA binding, and improved Hsp70 expression relative to non-REMFS-treated cells |
| 16168601 | Western blot analysis indicated that HSF1 but not HSF2 protein levels were reduced in aged donor samples |
| 10867642 | We have previously reported that osmotic stress prominently induces the DNA binding activity of the heat shock transcription factor 1 (HSF1) |
| 10867642 | In the present study, we examined the effects of medium osmolarity on both the activation of HSF1 and the programmed cell death in normal human fibroblasts during cellular senescence |
| 10867642 | The activation of HSF1 occurred rapidly in presenescent (early passage) IMR-90 cells when exposed to either hypo-osmotic or hyperosmotic stress |
| 10867642 | In contrast, the activation of HSF1 was significantly attenuated in senescent cells |
| 10867642 | Western blot analysis indicated that equal amounts of HSF1 were present as monomers in the cytoplasm of both presenescent and senescent cells in normal growth medium |
| 10867642 | Under either hypo-osmotic or hyperosmotic stress, trimerization and nuclear localization of HSF1 occurred in presenescent cells but not in senescent cells |
| 10867642 | More than 80% of HSF1 in senescent cells remained as monomers in the cytoplasm under osmotic stress, suggesting a defect in the signal transduction pathways that lead to HSF1 trimerization or a dysfunction in the HSF1 protein itself |
| 10867642 | All three MAPKs were activated by hyperosmotic stress but not hypo-osmotic stress, suggesting that the MAPK signal transduction pathways may not be directly linked to the osmotic stress-induced activation of HSF1 |
| 10867642 | Despite the prominent induction of HSF1 activation, the presenescent cells were more sensitive than the senescent cells to the osmotic stress-induced apoptosis |
| 9637782 | The binding activity of the heat shock transcription factor HSF1, as measured by a gel shift assay, was significantly higher in early passage cells and cells from young donors in comparison to late passage cells and cells from old donors |
| 9637782 | In addition, the levels of HSF1 decreased significantly in late passage cells and cells from old donors in comparison to early passage cells and cells from young donors |
| 9637782 | In addition, our study shows that the decline in hsp70 expression during cellular senescence in vitro and in cells derived from old human subjects is paralleled by a decrease in the levels of HSF1 |
| 9147375 | Inadequate promoter priming by the transactivator or heat shock genes, heat shock factor 1 (HSF1), is thought to account for age-dependent diminution in expression of these genes, although the exact mechanism for this loss is not clearly understood |
| 9147375 | Whole cell extracts from these donor cells have the capacity to inhibit HSF1-DNA binding when mixed with pre-activated HSF1 from HeLa cells |
| 8864063 | Analyses of the regulation and function of heat shock factor 1 (HSF1), a transcription factor that mediates the response to heat shock, showed that while the relative abundance of both the hsf1 transcript and the HSF1 protein did not change as a function of age, the responsiveness of HSF1 to heat-induced activation, as measured by its trimerization and ability to bind to the heat shock element consensus sequence, was inversely related to the age of the cells used |
| 8864063 | Given the fundamentally important role of heat shock proteins (HSPs) in many aspects of protein homeostasis and signal transduction it seems likely that the inability, or compromised ability, of aging cells and organisms to activate HSF1 and produce HSPs in response to stress would contribute to the well-known increase in morbidity and mortality of the aged when challenged |
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