Quercetin suppresses heat shock response by down regulation of HSF1 - PubMed (original) (raw)
. 1995 Mar 28;208(3):1099-105.
doi: 10.1006/bbrc.1995.1447.
Affiliations
- PMID: 7702609
- DOI: 10.1006/bbrc.1995.1447
Quercetin suppresses heat shock response by down regulation of HSF1
N Nagai et al. Biochem Biophys Res Commun. 1995.
Abstract
A bioflavonoid quercetin suppressed the stress response in heat-shocked cells and we have investigated the inhibitory mechanism in this report. After treatment of cells with nonlethal concentrations of quercetin, the binding of heat shock factor (HSF) to the heat shock element (HSE) was inhibited as detected by gel shift assay. We examined whether quercetin inhibits heat shock response by inhibiting HSF trimer-formation and found it was not the case. Instead, pretreatment of the cells with quercetin caused a decrease in the level of HSF1, especially of the constitutively phosphorylated form. This decrease was more prominent in heat-shocked cells than in control cells. These data suggest that (1) quercetin does not affect the trimer formation of HSF1, and (2) the decline of the HSF1-HSE complex might be linked to the decrease of HSF1 levels caused by quercetin.
Similar articles
- Distinct stress-inducible and developmentally regulated heat shock transcription factors in Xenopus oocytes.
Gordon S, Bharadwaj S, Hnatov A, Ali A, Ovsenek N. Gordon S, et al. Dev Biol. 1997 Jan 1;181(1):47-63. doi: 10.1006/dbio.1996.8441. Dev Biol. 1997. PMID: 9015264 - Quercetin inhibits heat shock protein induction but not heat shock factor DNA-binding in human breast carcinoma cells.
Hansen RK, Oesterreich S, Lemieux P, Sarge KD, Fuqua SA. Hansen RK, et al. Biochem Biophys Res Commun. 1997 Oct 29;239(3):851-6. doi: 10.1006/bbrc.1997.7572. Biochem Biophys Res Commun. 1997. PMID: 9367858 - Inhibiting the transcription factor HSF1 as an anticancer strategy.
Whitesell L, Lindquist S. Whitesell L, et al. Expert Opin Ther Targets. 2009 Apr;13(4):469-78. doi: 10.1517/14728220902832697. Expert Opin Ther Targets. 2009. PMID: 19335068 Review. - Regulation of thermotolerance and ischemic tolerance.
Nagata K. Nagata K. EXS. 1996;77:467-81. doi: 10.1007/978-3-0348-9088-5_31. EXS. 1996. PMID: 8856991 Review.
Cited by
- Histone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher disease.
Lu J, Yang C, Chen M, Ye DY, Lonser RR, Brady RO, Zhuang Z. Lu J, et al. Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):21200-5. doi: 10.1073/pnas.1119181109. Epub 2011 Dec 12. Proc Natl Acad Sci U S A. 2011. PMID: 22160715 Free PMC article. - Bortezomib-induced heat shock response protects multiple myeloma cells and is activated by heat shock factor 1 serine 326 phosphorylation.
Shah SP, Nooka AK, Jaye DL, Bahlis NJ, Lonial S, Boise LH. Shah SP, et al. Oncotarget. 2016 Sep 13;7(37):59727-59741. doi: 10.18632/oncotarget.10847. Oncotarget. 2016. PMID: 27487129 Free PMC article. - Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach.
Chatterjee S, Burns TF. Chatterjee S, et al. Int J Mol Sci. 2017 Sep 15;18(9):1978. doi: 10.3390/ijms18091978. Int J Mol Sci. 2017. PMID: 28914774 Free PMC article. Review. - HTS-compatible beta-lactamase transcriptional reporter gene assay for interrogating the heat shock response pathway.
Hancock MK, Xia M, Frey ES, Sakamuru S, Bi K. Hancock MK, et al. Curr Chem Genomics. 2009 Feb 5;3:1-6. doi: 10.2174/1875397300903010001. Curr Chem Genomics. 2009. PMID: 20161831 Free PMC article. - HSF1 as a Cancer Biomarker and Therapeutic Target.
Carpenter RL, Gökmen-Polar Y. Carpenter RL, et al. Curr Cancer Drug Targets. 2019;19(7):515-524. doi: 10.2174/1568009618666181018162117. Curr Cancer Drug Targets. 2019. PMID: 30338738 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources