HCSGD entry for HSPA4
1. General information
| Official gene symbol | HSPA4 |
|---|---|
| Entrez ID | 3308 |
| Gene full name | heat shock 70kDa protein 4 |
| Other gene symbols | APG-2 HS24/P52 HSPH2 RY hsp70 hsp70RY |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0005524 | ATP binding | NAS | molecular_function |
| GO:0005634 | Nucleus | IDA | cellular_component |
| GO:0005730 | Nucleolus | IDA | cellular_component |
| GO:0005737 | Cytoplasm | IDA | cellular_component |
| GO:0005739 | Mitochondrion | IDA | cellular_component |
| GO:0006986 | Response to unfolded protein | NAS | biological_process |
| GO:0045040 | Protein import into mitochondrial outer membrane | IDA | biological_process |
| GO:0051131 | Chaperone-mediated protein complex assembly | IDA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.0733452110 | 0.7149857262 | 0.5760942721 | 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 | 0.5320528233 |
| GSE13712_SHEAR | Up | 0.2751906466 |
| GSE13712_STATIC | Down | -0.0437346411 |
| GSE19018 | Down | -0.3361819908 |
| GSE19899_A1 | Up | 0.5895045770 |
| GSE19899_A2 | Up | 0.2669986359 |
| PubMed_21979375_A1 | Up | 0.0726434754 |
| PubMed_21979375_A2 | Up | 0.0684755647 |
| GSE35957 | Up | 0.0684560021 |
| GSE36640 | Up | 0.0101939462 |
| GSE54402 | Up | 0.2863970655 |
| GSE9593 | Up | 0.2079728639 |
| GSE43922 | Up | 0.2244859043 |
| GSE24585 | Down | -0.1658539438 |
| GSE37065 | Down | -0.0594340862 |
| GSE28863_A1 | Up | 0.2941689295 |
| GSE28863_A2 | Up | 0.6223541752 |
| GSE28863_A3 | Down | -0.4993796830 |
| GSE28863_A4 | Down | -0.2935932904 |
| GSE48662 | Down | -0.2475665590 |
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-1 | MIMAT0000416 | MIRT003977 | Luciferase reporter assay | Functional MTI | 17715156 |
| hsa-miR-30c-5p | MIMAT0000244 | MIRT007050 | Luciferase reporter assay//qRT-PCR | Functional MTI | 22842562 |
| hsa-miR-26b-5p | MIMAT0000083 | MIRT030164 | Microarray | Functional MTI (Weak) | 19088304 |
| hsa-miR-942-5p | MIMAT0004985 | MIRT036559 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-615-3p | MIMAT0003283 | MIRT039721 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-320a | MIMAT0000510 | MIRT044647 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-10a-5p | MIMAT0000253 | MIRT047525 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-148a-3p | MIMAT0000243 | MIRT048037 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-197-3p | MIMAT0000227 | MIRT048125 | CLASH | Functional MTI (Weak) | 23622248 |
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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: 22 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 27091568 | Recombinant HSP70 and mild heat shock stimulate growth of aged mesenchymal stem cells |
| 27091568 | We have shown earlier that prolonged administration of recombinant human HSP70 to mice exhibiting Alzheimer's-like neurodegeneration as well as during sepsis reduces the clinical manifestations of these pathologies |
| 27091568 | Herein, we studied the action of recombinant human HSP70 on young and aged mouse mesenchymal stem cells (MSCs) in culture |
| 27091568 | The results obtained indicate that HSP70 at concentrations of 2 mug/ml and higher significantly stimulates growth of aged but not young MSCs |
| 27091568 | Western blotting and protein labeling experiments demonstrated that neither mild heat shock nor exogenous HSP70 administration resulted in significant endogenous HSP70 induction in young and aged MSCs, whereas mild heat shock increased HSC70 levels in aged MSCs |
| 27091568 | The results of this study suggest that the administration of exogenous HSP70 and the application of mild heat stress may produce a certain "rejuvenating" effect on MSCs and possibly other cell types in vivo, and these interventions may potentially be used for life extension by delaying various manifestations of aging at the molecular and cellular level |
| 26865365 | Studies have linked the expression of HSP70s to several types of carcinoma, with Hsp70 expression being associated with therapeutic resistance, metastasis, and poor clinical outcome |
| 26865365 | ATP hydrolysis and adenosine diphosphate (ADP)/ATP exchange are key events for substrate binding and Hsp70 release during folding of nascent polypeptides |
| 26865365 | Several proteins that bind to distinct subdomains of Hsp70 and consequently modulate the activity of the chaperone have been identified as HSP70 co-chaperones |
| 26865365 | This review focuses on the regulation, function, and relevance of the molecular Hsp70 chaperone machinery to disease and its potential as a therapeutic target |
| 25292174 | Obesity depresses the anti-inflammatory HSP70 pathway, contributing to NAFLD progression |
| 25292174 | OBJECTIVES: To evaluate whether reduced activity of the anti-inflammatory HSP70 pathway correlates with nonalcoholic fatty liver disease (NAFLD) progression and with markers of oxidative stress because obesity activates inflammatory JNKs, whereas HSP70 exerts the opposite effect |
| 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 | The immunohistochemistry results suggested Kupffer cells as a site of HSP70 inhibition |
| 25292174 | CONCLUSIONS: Decreased HSF1 levels in the liver and fat of obese patients correlated with impairment of HSP70 in an NAFLD stage-dependent manner |
| 24997994 | Bag3 is a member of the BAG family of co-chaperones that interacts with Hsp70 |
| 23427299 | Further metabolic assays revealed significantly impaired mitochondrial function and hyperactive glycolysis, which were concomitant with the upregulation of HIF-1 and Hsp70 |
| 21681022 | BAG3 was recently described as a mediator of a novel macroautophagy pathway that uses the specificity of heat shock protein 70 (HSP70) to misfolded proteins and also involves other protein partners, such as HSPB8 |
| 19097133 | Induction of the heat shock response (HSR), determined by hsp70-luciferase reporter and HSP70 protein expression, is attenuated as a function of age of the IMR-90 human diploid fibroblasts |
| 18770009 | From proliferative to neurological role of an hsp70 stress chaperone, mortalin |
| 18575266 | Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10 |
| 18438428 | The chaperone, heat shock protein (Hsp)70, bound to both Bax and the mitochondrial apoptosis inducing factor following cytokine withdrawal, and impeded inhibitors of kappaB (IkappaB)-mediated inhibition of nuclear factor-kappaB anti-apoptotic signalling |
| 18438428 | Impairment of Hsp70 activity--using a pharmacological Hsp inhibitor or transfecting cells with an Hsp70-blocking antibody--restored the cellular response to mitochondrial apoptosis triggering |
| 18438428 | Thus, constitutive de-novo cyclin D1 production in B cells delays commitment to apoptosis by inducing Hsp70 chaperoning activity on pre- and post-mitochondrial pro-apoptotic factors |
| 18325704 | Furthermore, REMFS increased HSF1 phosphorylation, enhanced HSF1-DNA binding, and improved Hsp70 expression relative to non-REMFS-treated cells |
| 18262743 | Furthermore, all three modulators tested in the present study bring about their effects by inducing stress response pathways in terms of an increase in the levels of stress proteins Hsp90, Hsp70 and heme-oxygenase-1 (HO-1), which is indicative of stress-induced hormesis bringing about the biologically beneficial effects |
| 17460210 | Furthermore, these cells exhibit a significant extension of their proliferative life span, while they respond better to exogenous stress by producing significantly higher levels of heat-shock protein-70 (HSP70) |
| 16516887 | These interactions alter the localized state of chromatin compaction, subsequently affecting the expression of subsets of genes, including those associated with the stress response (Hsp70), apoptosis (Bax, MDM2) and cell cycle regulation (p21WAF1, cyclin B) in a cell- and tissue-specific manner |
| 16168601 | Nuclear run-on analysis revealed a 66% reduction in hsp70 transcription rates in old compared to young nuclei harvested from T-cells exposed to a brief 42 degrees C heat shock |
| 16168601 | To determine if one or more protein transactivators of the proximal and distal promoter regions of the hsp70 gene were affected by age, gel shift analysis was performed |
| 14980418 | The present study has been undertaken to test whether the growth of human BMSCs under the same conditions would translate into preservation of cellular aging-attenuated functions, such as the ability to express HSP70 in response to stress as well as of osteogenic differentiation potential |
| 14980418 | We report here that growth of BMSCs on a DC matrix versus tissue culture polystyrene significantly reduced one of the main manifestations of cellular aging, the attenuation of the ability to express a major protective stress response component, HSP70, increased the proliferation capacity of ex vivo expanded BMSCs, reduced the rate of morphological changes, and resulted in a dramatic increase in the retention of the potential to express osteogenic-specific functions and markers upon treatment with osteogenic stimulants |
| 12392764 | Finally, it has been recently demonstrated that in aged cells one of the key aging-related processes previously considered irreversible, attenuation of the expression of a major stress response protein, Hsp70, can be reversed |
| 12392764 | Indeed, in the present study, growth on a denatured collagen matrices reversed in aged cells not only the attenuation of Hsp70 expression but also other aging-related processes, such as beta-galactosidase expression, increase in protein oxidation and changes in cell morphology |
| 10502396 | We examined the effects of cellular aging on the expression of the heat shock-inducible HSP70 gene in WI-38 diploid human fibroblasts serially passaged in vitro |
| 10502396 | A marked decrease in the synthesis and accumulation of the inducible HSP70 protein was observed in serum-fed late passage cells exposed to a severe heat shock (30 min at 45 degrees C) in comparison to early passage cells |
| 10502396 | Similarly, Northern blotting analysis indicated that comparable amounts of inducible HSP70 mRNA were present in the total RNA fraction, in the total polyadenylated RNA fraction, or in the nuclear polyadenylated RNA fraction extracted from both early and late passage cells |
| 10502396 | In contrast, much less inducible HSP70 mRNA was detected in the total cytoplasmic RNA fraction or in the polyadenylated cytoplasmic RNA fraction of late passage cells |
| 10502396 | Thus age-related differences in heat-induced HSP70 synthesis and accumulation observed in serum-fed WI-38 cells appeared to result from an impairment in the posttranscriptional processing of the HSP70 mRNA at a level following the polyadenylation step and preceding translocation from the nucleus to the cytoplasm |
| 10502396 | When HF were serum deprived for 20 h before heat shock, the induction of HSP70 mRNA was less than 30% reduced in early passage cells in comparison to serum-fed cells; however, the level of HSP70 mRNA was markedly (over 80%) decreased in serum-deprived late passage cells |
| 10502396 | This result indicated that the presence of serum has a strong influence on heat shock-induced HSP70 gene expression in human fibroblasts aging in vitro |
| 9637782 | Because heat shock proteins have been shown to play a critical role in protecting cells from hyperthermia and other types of stresses, it was of interest to determine what effect cellular senescence in vitro and cells cultured in vitro from young and old human donors have on the ability of cells to regulate the expression of heat shock protein 70 (hsp70), the most prominent and most evolutionary conserved of the heat shock proteins |
| 9637782 | The ability of early and late passage IMR-90 lung fibroblasts and epidermal melanocytes and skin fibroblasts obtained from young and old human donors to express hsp70 was determined after a brief heat shock |
| 9637782 | We found that the levels of hsp70 protein and mRNA were lower in late passage cells and cells from old donors than in early passage cells and cells from young donors |
| 9637782 | Thus, our study demonstrates that the induction of hsp70 by hyperthermia in fibroblasts is significantly lower in late passage fibroblasts and in fibroblasts from old 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 |
| 7988669 | Hsp70 and aging |
| 7988669 | Using hepatocytes freshly isolated from young adult and old rats, we have shown that the induction of hsp70 expression by heat shock is reduced approximately 50% with age |
| 7988669 | The decrease in hsp70 expression occurs at the level of transcription and appears to arise from a defect in the heat shock transcription factor |
| 7988669 | Other investigators have also shown that the induction of hsp70 expression by heat shock as well as other stresses declines significantly with age in a variety of tissues from rats as well as mononuclear cells from human subjects |
| 7988669 | In addition, a decrease in the inducibility of hsp70 is observed with cell senescence in cultured cells |
| 7988669 | Therefore, it appears that a reduced ability to express hsp70 in response to stress may be a common phenomenon underlying the aging process |
| 1902836 | We examined the effect of cellular aging on adult mortality and hsp70 gene expression in Drosophila melanogaster under thermal stress |
| 1902836 | The level of hsp70 mRNA increases in flies up to 23-28 days of age, but then declines as they get older |
| 1902836 | When flies are shifted to 25 degrees C after 30 min of heat stress, the time-dependent decrease in hsp70 mRNA levels occurs more rapidly in young flies than in old ones |
| 1902836 | The hsp70 mRNA present during this recovery period is translated into protein, and senescent flies continue to synthesize this protein for up to 5 h after heat shock |
| 1902836 | The prolonged expression of hsp70 RNA during recovery from heat shock was also observed in young flies fed canavanine, an arginine analogue |
| 1902836 | These data suggest that in old insects, the accumulation of conformationally altered proteins plays a role in the regulation of hsp70 RNA expression |
| 2632278 | We present examples of four types of alterations which contribute to the senescence phenotype of WI-38 cells: a) in senescent cells there is an increased lability of the tyrosine autophosphorylation capacity of detergent isolated EGF receptor; b) following serum stimulation, the calmodulin protein level fails to increase in senescent cells, although the calmodulin mRNA level increases as expected; c) following heat shock at 43 degrees C, senescent cells produce both less RNA and less protein for the HSP70 and HSP90 genes; d) we find that membranes isolated in basic buffer from senescent or young cells increase the EGF proliferative response of senescing cells, in contrast to the finding by others that membranes isolated in neutral buffer inhibit cell proliferation (Pereira-Smith et al |
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