Role of Heat Shock Factor 1 in Neural Development and Disorders

2020 ◽  
Author(s):  
Dipankar J. Dutta ◽  
Kazue Hashimoto-Torii ◽  
Masaaki Torii
Keyword(s):  
Heat Shock ◽  
Neural Development ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1

The possible role of heat shock factor-1 in the negative regulation of heme oxygenase-1

2005 ◽  
Vol 37 (3) ◽  
pp. 604-615 ◽  
Author(s):  
Yenn-Hwei Chou ◽  
Feng-Ming Ho ◽  
Der-Zen Liu ◽  
Shyr-Yi Lin ◽  
Li-Hsueh Tsai ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heme Oxygenase ◽  
Heat Shock Factor ◽  
Negative Regulation ◽  
Heme Oxygenase 1 ◽  
Heat Shock Factor 1

Role of Heat Shock Factor 1 in HIV

2020 ◽  
Author(s):  
Xinfeng Xu ◽  
Xiaoyan Pan ◽  
Shuwen Liu
Keyword(s):  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1

scholarly journals The central role of heat shock factor 1 in synaptic fidelity and memory consolidation

2016 ◽  
Vol 21 (5) ◽  
pp. 745-753 ◽  
Author(s):  
Philip L. Hooper ◽  
Heather D. Durham ◽  
Zsolt Török ◽  
Paul L. Hooper ◽  
Tim Crul ◽  
...  
Keyword(s):  
Heat Shock ◽  
Memory Consolidation ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1

Role of heat shock factor 1 expression in the microenvironment of intrahepatic cholangiocarcinomas

2018 ◽  
Vol 33 (7) ◽  
pp. 1407-1412
Author(s):  
Yoichiro Kawashita ◽  
Yuji Morine ◽  
Yu Saito ◽  
Chie Takasu ◽  
Tetsuya Ikemoto ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Intrahepatic Cholangiocarcinomas

Poly(ADP-ribosyl)ation regulates heat shock factor-1 activity and the heat shock response in murine fibroblasts

2006 ◽  
Vol 84 (5) ◽  
pp. 703-712 ◽  
Author(s):  
Silvia Fossati ◽  
Laura Formentini ◽  
Zhao-Qi Wang ◽  
Flavio Moroni ◽  
Alberto Chiarugi
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Mammalian Cells ◽  
Molecular Mechanisms ◽  
Heat Shock Factor ◽  
Binding Motif ◽  
Heat Shock Factor 1 ◽  
Shock Response ◽  
Parp 1

Poly(ADP-ribose) polymerase-1 (PARP-1)-dependent poly(ADP-ribose) formation is emerging as a key regulator of transcriptional regulation, even though the targets and underlying molecular mechanisms have not yet been clearly identified. In this study, we gathered information on the role of PARP-1 activity in the heat shock response of mouse fibroblasts. We show that DNA binding of heat shock factor (HSF)-1 was impaired by PARP-1 activity in cellular extracts, and was higher in PARP-1−/− than in PARP-1+/+ cells. No evidence for HSF-1 poly(ADP-ribosyl)ation or PARP-1 interaction was found, but a poly(ADP-ribose) binding motif was identified in the transcription factor amino acid sequence. Consistent with data on HSF-1, the expression of heat-shock protein (HSP)-70 and HSP–27 was facilitated in cells lacking PARP-1. Thermosensitivity, however, was higher in PARP-1−/− than in PARP-1+/+ cells. Accordingly, we report that heat-shocked PARP-1 null fibroblasts showed an increased activation of proapoptotic JNK and decreased transcriptional efficiency of prosurvival NF-κB compared with wild-type counterparts. The data indicate that poly(ADP-ribosyl)ation finely regulates HSF-1 activity, and emphasize the complex role of PARP-1 in the heat-shock response of mammalian cells.

scholarly journals Role of heat shock factor-1 activation in the doxorubicin-induced heart failure in mice

2010 ◽  
Vol 298 (6) ◽  
pp. H1832-H1841 ◽  
Author(s):  
Kaushik Vedam ◽  
Yoshinori Nishijima ◽  
Lawrence J. Druhan ◽  
Mahmood Khan ◽  
Nicanor I. Moldovan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heart Failure ◽  
Heat Shock ◽  
Mrna Level ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Knock Out ◽  
Apoptotic Protein ◽  
Shock Proteins

Treating cancer patients with chemotherapeutics, such as doxorubicin (Dox), cause dilated cardiomyopathy and congestive heart failure because of oxidative stress. On the other hand, heat shock factor-1 (HSF-1), a transcription factor for heat shock proteins (Hsps), is also known to be activated in response to oxidative stress. However, the possible role of HSF-1 activation and the resultant Hsp25 in chemotherapeutic-induced heart failure has not been investigated. Using HSF-1 wild-type (HSF-1+/+) and knock-out (HSF-1−/−) mice, we tested the hypothesis that activation of HSF-1 plays a role in the development of Dox-induced heart failure. Higher levels of Hsp25 and its phosphorylated forms were found in the failing hearts of Dox-treated HSF-1+/+ mice. More than twofold increase in Hsp25 mRNA level was found in Dox-treated hearts. Proteomic analysis showed that there is accumulation and aggregation of Hsp25 in Dox-treated failing hearts. Additionally, Hsp25 was found to coimmunoprecipitate with p53 and vice versa. Further studies indicated that the Dox-induced higher levels of Hsp25 transactivated p53 leading to higher levels of the pro-apoptotic protein Bax, but other p53-related proteins remained unaltered. Moreover, HSF-1−/− mice showed significantly reduced Dox-induced heart failure and higher survival rate, and there was no change in Bax upon treating with Dox in HSF-1−/− mice. From these results we propose a novel mechanism for Dox-induced heart failure: increased expression of Hsp25 because of oxidant-induced activation of HSF-1 transactivates p53 to increase Bax levels, which leads to heart failure.

Heat-shock factor 1 both positively and negatively affects cellular clonogenic growth depending on p53 status

2013 ◽  
Vol 452 (2) ◽  
pp. 321-329 ◽  
Author(s):  
Chau H. Nguyen ◽  
Benjamin J. Lang ◽  
Ryan C. C. Chai ◽  
Jessica L. Vieusseux ◽  
Michelle M. Kouspou ◽  
...  
Keyword(s):  
Heat Shock ◽  
Cancer Cell ◽  
Heat Shock Factor ◽  
Mutant P53 ◽  
Heat Shock Factor 1 ◽  
Dependent Manner ◽  
Wild Type ◽  
Clonogenic Growth ◽  
Wild Type P53

HSF1 (heat-shock factor 1) is the master regulator of the heat-shock response; however, it is also activated by cancer-associated stresses and supports cellular transformation and cancer progression. We examined the role of HSF1 in relation to cancer cell clonogenicity, an important attribute of cancer cells. Ectopic expression or HSF1 knockdown demonstrated that HSF1 positively regulated cancer cell clonogenic growth. Furthermore, knockdown of mutant p53 indicated that HSF1 actions were mediated via a mutant p53-dependent mechanism. To examine this relationship more specifically, we ectopically co-expressed mutant p53R273H and HSF1 in the human mammary epithelial cell line MCF10A. Surprisingly, within this cellular context, HSF1 inhibited clonogenicity. However, upon specific knockdown of endogenous wild-type p53, leaving mutant p53R273H expression intact, HSF1 was observed to greatly enhance clonogenic growth of the cells, indicating that HSF1 suppressed clonogenicity via wild-type p53. To confirm this we ectopically expressed HSF1 in non-transformed and H-RasV12-transformed MCF10A cells. As expected, HSF1 significantly reduced clonogenicity, altering wild-type p53 target gene expression levels consistent with a role of HSF1 increasing wild-type p53 activity. In support of this finding, knockdown of wild-type p53 negated the inhibitory effects of HSF1 expression. We thus show that HSF1 can affect clonogenic growth in a p53 context-dependent manner, and can act via both mutant and wild-type p53 to bring about divergent effects upon clonogenicity. These findings have important implications for our understanding of HSF1's divergent roles in cancer cell growth and survival as well as its disparate effect on mutant and wild-type p53.

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