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Shinkawa T Tan K Fujimoto M Hayashida N Yamamoto K Takaki E Takii R Prakasam R Inouye S Mezger V Nakai A 《Molecular biology of the cell》2011,22(19):3571-3583
Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs. However, the fundamental roles of HSF2 in vertebrate cells have not been identified. Here we find that vertebrate HSF2 is activated during heat shock in the physiological range. HSF2 deficiency reduces threshold for chicken HSF3 or mouse HSF1 activation, resulting in increased HSP expression during mild heat shock. HSF2-null cells are more sensitive to sustained mild heat shock than wild-type cells, associated with the accumulation of ubiquitylated misfolded proteins. Furthermore, loss of HSF2 function increases the accumulation of aggregated polyglutamine protein and shortens the lifespan of R6/2 Huntington's disease mice, partly through αB-crystallin expression. These results identify HSF2 as a major regulator of proteostasis capacity against febrile-range thermal stress and suggest that HSF2 could be a promising therapeutic target for protein-misfolding diseases. 相似文献
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Federica Rossin Valeria Rachela Villella Manuela D'Eletto Maria Grazia Farrace Speranza Esposito Eleonora Ferrari Romina Monzani Luca Occhigrossi Vittoria Pagliarini Claudio Sette Giorgio Cozza Nikolai A Barlev Laura Falasca Gian Maria Fimia Guido Kroemer Valeria Raia Luigi Maiuri Mauro Piacentini 《EMBO reports》2018,19(7)
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A novel HSF1-mediated death pathway that is suppressed by heat shock proteins 总被引:6,自引:0,他引:6
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Hayashida N Inouye S Fujimoto M Tanaka Y Izu H Takaki E Ichikawa H Rho J Nakai A 《The EMBO journal》2006,25(20):4773-4783
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Katsuki K Fujimoto M Zhang XY Izu H Takaki E Tanizawa Y Inouye S Nakai A 《FEBS letters》2004,571(1-3):187-191
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Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage 总被引:19,自引:0,他引:19
In this study, using heat shock factor 1 (Hsf1) knockout mice as a model, we tested the hypothesis that HSF1-dependent regulation of heat shock proteins (Hsps) is required to maintain redox state and attenuate oxidative damage in the normal heart. Here we report that, in mice, HSF1 deficiency reduces cardiac expression of Hsp25, alphaB-crystallin and Hsp70, but not Hsp60 and Hsp90. Consistent with the downregulation of Hsp25, for example, a significantly lower glutathione (GSH)/glutathione disulfate (GSSG) ratio was associated with the decreased activity, but not protein content, of glucose 6-phosphate dehydrogenase. Con sequently, superoxide was generated at a higher rate, and several mitochondrial proteins, including adenine nucleotide translocase 1 (ANT1), were more oxidized by HSF1 deficiency in vivo. Oxidative damage to ANT1 protein, a structural component of the mitochondrial permeability transition pore (MPTP), decreases its catalytic activity and increases MPTP opening, respectively. Taken together, our results indicate for the first time that constitutive expression of HSP chaperones requires HSF1 activity, and that such HSF1-dependent requirements are directly and functionally linked to maintain redox homeostasis and antioxidative defenses at normal (37 degrees C) temperature. 相似文献
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