scholarly journals Upregulation of lactate dehydrogenase A by ErbB2 through heat shock factor 1 promotes breast cancer cell glycolysis and growth

Oncogene ◽  
2009 ◽  
Vol 28 (42) ◽  
pp. 3689-3701 ◽  
Author(s):  
Y H Zhao ◽  
M Zhou ◽  
H Liu ◽  
Y Ding ◽  
H T Khong ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Lactate Dehydrogenase ◽  
Heat Shock ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1

Concurrent Exposure to Heat Shock and H7 Synergizes to Trigger Breast Cancer Cell Apoptosis while Sparing Normal Cells

2003 ◽  
Vol 77 (3) ◽  
pp. 233-243 ◽  
Author(s):  
Wenle Xia ◽  
Lys Hardy ◽  
Leihua Liu ◽  
Sumin Zhao ◽  
Mark Goodman ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Heat Shock ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Cell Apoptosis ◽  
Normal Cells ◽  
Cancer Cell Apoptosis

scholarly journals Drugging the heat shock factor 1 pathway: Exploitation of the critical cancer cell dependence on the guardian of the proteome

Cell Cycle ◽  
2009 ◽  
Vol 8 (23) ◽  
pp. 3806-3808 ◽  
Author(s):  
Emmanuel de Billy ◽  
Marissa V. Powers ◽  
Jennifer R. Smith ◽  
Paul Workman
Keyword(s):  
Heat Shock ◽  
Cancer Cell ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
The Guardian

scholarly journals Heat shock factor 1 confers resistance to lapatinib in ERBB2-positive breast cancer cells

2018 ◽  
Vol 9 (6) ◽  
Author(s):  
Alisha Yallowitz ◽  
Amr Ghaleb ◽  
Lucas Garcia ◽  
Evguenia M. Alexandrova ◽  
Natalia Marchenko
Keyword(s):  
Breast Cancer ◽  
Heat Shock ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Positive Breast Cancer

scholarly journals Heat Shock Factor 1 (HSF1) cooperates with estrogen receptor α (ERα) in the regulation of estrogen action in breast cancer cells

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Natalia Vydra ◽  
Patryk Janus ◽  
Paweł Kuś ◽  
Tomasz Stokowy ◽  
Katarzyna Mrowiec ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Heat Shock ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Estrogen Receptor Α ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Er Positive ◽  
Positive Breast Cancer

Heat shock factor 1 (HSF1), a key regulator of transcriptional responses to proteotoxic stress, was linked to estrogen (E2) signaling through estrogen receptor α (ERα). We found that an HSF1 deficiency may decrease ERα level, attenuate the mitogenic action of E2, counteract E2-stimulated cell scattering, and reduce adhesion to collagens and cell motility in ER-positive breast cancer cells. The stimulatory effect of E2 on the transcriptome is largely weaker in HSF1-deficient cells, in part due to the higher basal expression of E2-dependent genes, which correlates with the enhanced binding of unliganded ERα to chromatin in such cells. HSF1 and ERα can cooperate directly in E2-stimulated regulation of transcription, and HSF1 potentiates the action of ERα through a mechanism involving chromatin reorganization. Furthermore, HSF1 deficiency may increase the sensitivity to hormonal therapy (4-hydroxytamoxifen) or CDK4/6 inhibitors (palbociclib). Analyses of data from the TCGA database indicate that HSF1 increases the transcriptome disparity in ER-positive breast cancer and can enhance the genomic action of ERα. Moreover, only in ER-positive cancers, an elevated HSF1 level is associated with metastatic disease.

scholarly journals DYRK2 activates heat shock factor 1 promoting resistance to proteotoxic stress in triplenegative breast cancer

2019 ◽  
Author(s):  
Rita Moreno ◽  
Sourav Banerjee ◽  
Angus W. Jackson ◽  
Jean Quinn ◽  
Gregg Baillie ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Heat Shock ◽  
Cancer Progression ◽  
Xenograft Model ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Proteotoxic Stress ◽  
Dual Specificity ◽  
Stress Response Pathway ◽  
Nuclear Stability

SummaryTo survive aneuploidy-induced proteotoxic stress, cancer cells activate the proteotoxic-stress response pathway, which is controlled by heat shock factor 1 (HSF1). This pathway supports cancer initiation, cancer progression and chemoresistance and thus is an attractive target. As developing HSF1 inhibitors is challenging, the identification and targeting of upstream regulators of HSF1 presents a tractable alternative strategy. Here we demonstrate that in triple negative breast cancer (TNBC) cells, the dual-specificity tyrosine-regulated kinase 2 (DYRK2) phosphorylates HSF1, promoting its nuclear stability and transcriptional activity. Thus, DYRK2 depletion reduces HSF1 activity and sensitises TNBC cells to proteotoxic stress. Importantly, in tumours from TNBC patients, DYRK2 levels positively correlate with active HSF1 and associates with poor prognosis, suggesting that DYRK2 could be promoting TNBC. In agreement with this, DYRK2 depletion reduces tumour growth in a TNBC xenograft model. These findings identify DYRK2 as both, a key modulator of the HSF1 transcriptional program, and a potential therapeutic target.

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