Heat stress (H + W) induced a slight increase in the expression level of both HSF3 and HSF1
. This effect was significantly increased when blue light was applied during heat stress (H + B).
HSP90 is one of the heat shock proteins reported to function as multichaperone complexes by combining with different cochaperones (Cdc37, p23, Hop, pP5, SGT1, Aha 1, etc.) affecting binding ability of HSP90 to client proteins (AKT, KIT, ErbB2, CDK 4, HSF1
, Apaf-1, MMp2, etc.) .
Overexpression of HSP-70 inhibits the phosphorylation of HSF1
by activating protein phosphatase and inhibiting protein kinase C activity.
"plays a crucial role in the response of brain cells to prenatal environmental insults," the researchers reported.
Both Hsps regulate the activation of the HSF1
transcription factor, which is linked to the transcriptional stress response [33, 34].
Induction of heat shock proteins by hyperthermia and noise overstimulation in hsf1
The member of the Hsf family, Hsf1
is involved in the Hsps induction owed to heat shock and other kinds of stress (8-10).
The gene, called heat-shock factor 1 (Hsf1
), doesn't itself trigger cancer.
In addition, decreases in ATP levels have been previously found to elicit the induction of HSPs by DNA binding and activation of the transcriptional factor HSF1
In NAFLD&NASH, we observed that oxidative stress could activate epidermal growth factor receptor (EGFR) to facilitate (i) UBC to repress HSF1
in the WNT and MAPK signaling pathways; (ii) APP to activate ETS1 in the MAPK signaling pathway to induce DNA repair function through the mediation of RFC5, to activate metabolism through the mediation of TRMT1, and to inhibit apoptosis through the mediation of ZNF480; and (iii) SHC1 to repress STAT5A in the MAPK signaling pathway.