Search bioRxiv⌕ Search

Biology subjects

Widlak, W.

Publications and source records attributed to Widlak, W..

3 recordsLinked to original sources

PDCD1 expression increases at elevated temperatures.

PDCD1 (Programmed cell death protein 1) is an immune checkpoint that inhibits the excessive response of antigen-activated T cells to prevent autoimmune tissue damage. In chronic infections or cancers, lasting antigen exposure leads to permanent PDCD1 expression that can limit immune-mediated clearance of pathogens or degenerated cells. Consequently, blocking PDCD1 can enhance T cell function, which is the basis of cancer immune checkpoint therapy. We found that PDCD1 expression can increase within hours of temperature elevation in human leukemic and lymphoblastoid cell lines (such as Jurkat, THP1, HL-60, GM07062, and NK-92) and mouse lymphoid organs (e.g., thymus, spleen, and lymph nodes). Transcriptional upregulation of the PDCD1 gene was associated with the binding of heat shock factor 1 (HSF1) to the promoter, and HSF1 knockout in HL-60 cells resulted in reduced PDCD1 activation. Furthermore, a heat shock-dependent increase in glycosylated (and therefore active) PDCD1 protein levels was associated with PDCD1 exposure on the cell membrane and a reduction in the cytotoxic properties of NK-92 cells. Our observations suggest that the immune response could be attenuated in various physiological conditions accompanied by increased temperatures (infection, heat stroke, etc.). This observation may have clinical implications, and therefore, further research is warranted to understand the importance of fever and PDCD1 in various disease states, as well as their interaction with treatment.

immunology↗

Heat Shock Factor 1 (HSF1) as a new tethering factor for ESR1 supporting its action in breast cancer.

Heat shock factor 1 (HSF1), a key regulator of transcriptional responses to proteotoxic stress, was recently linked to estrogen (E2) signaling through ESR1. We found that an HSF1 deficiency could lead to the inhibition of the mitogenic action of E2 in breast cancer cells. The stimulatory effect of E2 on the transcriptome is 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 ESR1 to chromatin. HSF1 and ESR1 can cooperate directly in E2-stimulated regulation of transcription, and HSF1 potentiates the action of ESR1 through a mechanism involving chromatin reorganization. Analyses of data from the TCGA database indicate that HSF1 increases the transcriptome diversity in ER-positive breast cancer and can enhance the genomic action of ESR1. Moreover, ESR1 and HSF1 are only prognostic when analyzed together (the worst prognosis for ER-/HSF1high cancers).

cancer biology↗

Heat shock response pathways regulate stimulus-specificity and sensitivity of NF-κB signalling to temperature stress

Ability to adapt to temperature changes trough the Heat Shock Response (HSR) pathways is one of the most fundamental and clinically relevant cellular response systems. Here we report that Heat Shock (HS) induces a temporally-coordinated and stimulus-specific adaptation of the signalling and gene expression responses of the Nuclear Factor {kappa}B (NF-{kappa}B) transcription factor. We show that exposure of MCF7 breast adenocarcinoma cells to 43{degrees}C 1h HS inhibits the immediate signalling response to pro-inflammatory Interleukin 1{beta} (IL1{beta}) and Tumour Necrosis Factor (TNF) cytokines. Within 4h after HS treatment IL1{beta}-induced responses return to normal levels, but the recovery of the TNF-induced responses is delayed. Using siRNA knock-down of Heat Shock Factor 1 and mathematical modelling we show that the stimulus-specificity is conferred via the Inhibitory {kappa}B kinase signalosome, with HSR differentially controlling individual cytokine transduction pathways. Finally, using a novel mathematical model we predict and experimentally validate that the HSR cross-talk confers differential cytokine sensitivity of the NF-{kappa}B system to a range of physiological and clinically-relevant temperatures. This quantitative understanding of NF-{kappa}B and HSR cross-talk mechanisms is fundamentally important for the potential improvement of current hyperthermia protocols.

cell biology↗