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Causes of lower induction of Hsp70 in neurons during heat shock are still a matter of debate. To further inquire into the mechanisms regulating Hsp70 expression in neurons, we studied the activity of Heat Shock Factor 1 (HSF1) and histone posttranslational modifications (PTMs) at the  hsp70  promoter in rat cortical neurons. Heat shock induced a transient and efficient translocation of HSF1 to neuronal nuclei. However, no binding of HSF1 at the  hsp70  promoter was detected while it bound to the  hsp25  promoter in cortical neurons during heat shock. Histone PTMs analysis showed that the  hsp70  promoter harbors lower levels of histone H3 and H4 acetylation in cortical neurons compared to PC12 cells under basal conditions. Transcriptomic profiling data analysis showed a predominant usage of cryptic transcriptional start sites at  hsp70  gene in the rat cerebral cortex, compared with the whole brain. These data support a weaker activation of  hsp70  canonical promoter. Heat shock increased H3Ac at the  hsp70  promoter in PC12 cells, which correlated with increased Hsp70 expression while no modifications occurred at the  hsp70  promoter in cortical neurons. Increased histone H3 acetylation by Trichostatin A led to  hsp70  mRNA and protein induction in cortical neurons. In conclusion, we found that two independent mechanisms maintain a lower induction of Hsp70 in cortical neurons. First, HSF1 fails to bind specifically to the  hsp70  promoter in cortical neurons during heat shock and, second, the  hsp70  promoter is less accessible in neurons compared to non-neuronal cells due to histone deacetylases repression.

plos one

Characterizing HSF1 Binding and Post-Translational Modifications of hsp70 Promoter in Cultured Cortical Neurons: Implications in the Heat-Shock Response