Interaction between Heat Shock Transcription Factors (HSFs) and Divergent Binding Sequences

Sakurai, Hiroshi; Takemori, Yukiko

doi:10.1074/jbc.m611801200

Cited by 45 publications

(48 citation statements)

References 63 publications

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“…Sakurai and Takemori (2007) noted that targets of HSF included cis-HSE sequences, which are the reverse repetitive sequences of multiple 5'-nGAAn-3'. HSF binding to HSEs is very important in HSP gene transcription, indicating that HSP gene transcription is regulated by the HSF gene.…”

Section: Discussionmentioning

confidence: 99%

Alteration of HSF3 and HSP70 mRNA expression in the tissues of two chicken breeds during acute heat stress

Zhang¹,

Kong²,

Zhang³

et al. 2014

Genet. Mol. Res.

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ABSTRACT. This study aimed to estimate changes in HSF3 and HSP70 mRNA expression in stress-sensitive tissues of 2 chicken breeds during acute heat stress. Lingshan chickens (LSC) and White Recessive Rock (WRR) (24 chickens of each breed) were randomly divided into 4 groups (0, 2, 3, and 6 h of heat treatment). With increasing heat treatment time, both HSF3 and HSP70 expression first declined and then showed a significant increase in both breeds. However, HSP70 expression decreased in the heart following 6 h of heat treatment, whereas HSF3 expression continued to increase. After 2 h of heat treatment, HSF3 expression was significantly higher in the brain and leg muscle of LSC compared to WRR (P < 0.05, P < 0.01). In comparison, HSP70 expression was significantly higher in the liver and leg muscle of WRR compared to LSC (P < 0.01, P < 0.05). After 3 h of heat treatment, HSF3 expression was significantly higher in the brain and leg muscle of LSC compared to WRR (P < 0.01). In comparison, HSP70 expression was significantly higher in the liver and heart of LSC compared to WRR (P < 0.01). These results indicate that the expression of HSF3 and HSP70 mRNA in LSC and WRR exhibit species-specific and tissue-specific differences during heat treatment.

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Section: Discussionmentioning

confidence: 99%

Alteration of HSF3 and HSP70 mRNA expression in the tissues of two chicken breeds during acute heat stress

Zhang¹,

Kong²,

Zhang³

et al. 2014

Genet. Mol. Res.

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“…It has beeen reported that the HSE and its binding protein heat shock transcription factor are highly conserved from yeast to humans. [19][20][21] It is well known that heat shock and hydrogen peroxide induces catalase gene expression in Aspergilli 5,[22][23][24] and other species, [6][7][8]25) and that each catalase gene promoter has regulatory element for stress response. But the regulatory elements are different in species.…”

Section: Discussionmentioning

confidence: 99%

Deletion Analysis of the Catalase-Encoding Gene (catB) Promoter fromAspergillus oryzae

Hisada

Sano

Hata

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…To test for the effects of riluzole on the turnover/decay of the 35 S-labeled cellular proteins, it was added to designated plates to a final concentration of 2 M at the beginning of the chase. Aliquots (in quadruplicate) of the cell culture medium were removed at 2, 4, 6, and 24 h after initiation of the chase, and the amount of trichloroacetic acid soluble radioactivity was determined according to published methods (19).…”

Section: Methodsmentioning

confidence: 99%

“…GLT1 was probed with either sc-15317 (1:200 dilution; SCBT) or ab61859 (1:500 dilution; Abcam); both gave similar results, although the Abcam antibody gave a lower background. To affirm even loading of protein, membrane was co-probed for actin (42 kDa) 35 S-labeled HSF1, it was added to designated plates to a final concentration of 2 M at the beginning of the chase. Cells were harvested at 0, 4,8,12, and 24 h after initiation of the chase in the absence versus the presence of 2 M riluzole.…”

Section: Methodsmentioning

confidence: 99%

Neuroprotective Drug Riluzole Amplifies the Heat Shock Factor 1 (HSF1)- and Glutamate Transporter 1 (GLT1)-dependent Cytoprotective Mechanisms for Neuronal Survival

Liu

Mathur

Mei

et al. 2011

Journal of Biological Chemistry

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Heat shock factor 1 (HSF1) mediates the cellular response to stress to increase the production of heat shock protein (HSP) chaperones for proper protein folding, trafficking, and degradation; failure of this homeostatic mechanism likely contributes to neurodegeneration. We show that the neuroprotective drug riluzole increased the amount of HSF1 in NG108-15 neuroprogenitor cells by slowing the specific turnover of HSF1 and supporting a more robust and sustained activation of HSF1. Using Hsp70-luciferase as a functional readout of the activity of HSF1, we show that riluzole amplified the heat shock induction of the reporter gene with an optimal increase at 1 M. Immunocytochemical staining and Western blot quantitation of HSP70 in NG108-15 neuroprogenitor cells and embryonic spinal cord neurons provided corroborative evidence that riluzole amplified the HSF1-dependent regulation of HSP70 expression. Parallel studies on the GLT1 glutamate transporter showed that riluzole increased GLT1-reporter and GLT1 protein expression and that the increase was enhanced by heat shock and coincident with the increased expression of HSP70 and HSP90. This result is consistent with the anti-glutamatergic profile of riluzole and the presence of multiple heat shock elements on the GLT1 gene promoter, suggesting that riluzole may modulate GLT1 expression through HSF1. The increased HSP chaperones and GLT1 transporter blunted glutamate-induced and N-methyl D-aspartate receptor-mediated excitotoxic death. In summary, we show that riluzole increased the amount and activity of HSF1 to boost the expression of HSPs and GLT1 for neuroprotection under stress.Induction of the heat shock response (HSR 2 ; also known as stress response) is a universally important quality control mechanism in protein homeostasis; it is a primary and evolutionarily conserved response to diverse stressors, mediated by activation of the HSF1 transcription factor, culminating in the induction of a family of heat shock proteins (HSPs) that function as chaperones to assist in the proper folding of non-native proteins and proteases to help in the degradation of damaged proteins for the protection and recovery from cellular damages (1-3). The biological importance of HSR is underscored by genetic evidence linking stress and protein homeostasis with the health and life span of the organism (4 -6) and by the increasing appreciation that problems in protein folding and aggregation likely contribute to the pathogenesis of a number of age-dependent neurodegenerative diseases that include amyotrophic lateral sclerosis (ALS), Huntington, Parkinson, Alzheimer, and prion diseases (6 -10).We are interested in harnessing the cytoprotective activity of HSR/HSF1 to promote cell survival under stress. In particular, we are interested in identifying agents that are not overtly proteotoxic and would not by themselves induce a robust HSR but would amplify the HSR and enhance the expression of HSPs. Riluzole is the only Food and Drug Administration-approved drug for ALS. The mode of action ...

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Interaction between Heat Shock Transcription Factors (HSFs) and Divergent Binding Sequences

Cited by 45 publications

References 63 publications

Alteration of HSF3 and HSP70 mRNA expression in the tissues of two chicken breeds during acute heat stress

Alteration of HSF3 and HSP70 mRNA expression in the tissues of two chicken breeds during acute heat stress

Deletion Analysis of the Catalase-Encoding Gene (catB) Promoter fromAspergillus oryzae

Neuroprotective Drug Riluzole Amplifies the Heat Shock Factor 1 (HSF1)- and Glutamate Transporter 1 (GLT1)-dependent Cytoprotective Mechanisms for Neuronal Survival

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