During ischemia-reperfusion in rat kidneys, heat shock response is not regulated by expressional changes of heat shock factor 1

SUMMARYThe intracellular build-up of thermally damaged proteins following exposure to heat stress results in the synthesis of a family of evolutionarily conserved proteins called heat shock proteins (Hsps) that act as molecular chaperones, protecting the cell against the aggregation of denatured proteins. The transcriptional regulation of heat shock genes by heat shock factor 1(HSF1) has been extensively studied in model systems, but little research has focused on the role HSF1 plays in Hsp gene expression in eurythermal organisms from broadly fluctuating thermal environments. The threshold temperature for Hsp induction in these organisms shifts with the recent thermal history of the individual but the mechanism by which this plasticity in Hsp induction temperature is achieved is unknown. We examined the effect of thermal acclimation on the heat-activation of HSF1 in the eurythermal teleost Gillichthys mirabilis. After a 5-week acclimation period (at 13, 21 or 28°C) the temperature of HSF1 activation was positively correlated with acclimation temperature. HSF1 activation peaked at 27°C in fish acclimated to 13°C, at 33°C in the 21°C group, and at 36°C in the 28°C group. Concentrations of both HSF1 and Hsp70 in the 28°C group were significantly higher than in the colder acclimated fish. Plasticity in HSF1 activation may be important to the adjustable nature of the heat shock response in eurythermal organisms and the environmental control of Hsp gene expression.

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Heat shock factor 1-independent activation of dendritic cells by heat shock: implication for the uncoupling of heat-mediated immunoregulation from the heat shock response

European Journal of Immunology ◽

10.1002/eji.200323687 ◽

2003 ◽

Vol 33 (6) ◽

pp. 1754-1762 ◽

Cited By ~ 20

Author(s):

Hong Zheng ◽

Ivor J Benjamin ◽

Sreyashi Basu ◽

Zihai Li

Keyword(s):

Dendritic Cells ◽

Heat Shock ◽

Heat Shock Response ◽

Heat Shock Factor ◽

Heat Shock Factor 1 ◽

Shock Response

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Poly(ADP-ribosyl)ation regulates heat shock factor-1 activity and the heat shock response in murine fibroblasts

Biochemistry and Cell Biology ◽

10.1139/o06-083 ◽

2006 ◽

Vol 84 (5) ◽

pp. 703-712 ◽

Cited By ~ 14

Author(s):

Silvia Fossati ◽

Laura Formentini ◽

Zhao-Qi Wang ◽

Flavio Moroni ◽

Alberto Chiarugi

Keyword(s):

Heat Shock ◽

Heat Shock Response ◽

Mammalian Cells ◽

Molecular Mechanisms ◽

Heat Shock Factor ◽

Binding Motif ◽

Heat Shock Factor 1 ◽

Shock Response ◽

Parp 1

Poly(ADP-ribose) polymerase-1 (PARP-1)-dependent poly(ADP-ribose) formation is emerging as a key regulator of transcriptional regulation, even though the targets and underlying molecular mechanisms have not yet been clearly identified. In this study, we gathered information on the role of PARP-1 activity in the heat shock response of mouse fibroblasts. We show that DNA binding of heat shock factor (HSF)-1 was impaired by PARP-1 activity in cellular extracts, and was higher in PARP-1−/− than in PARP-1+/+ cells. No evidence for HSF-1 poly(ADP-ribosyl)ation or PARP-1 interaction was found, but a poly(ADP-ribose) binding motif was identified in the transcription factor amino acid sequence. Consistent with data on HSF-1, the expression of heat-shock protein (HSP)-70 and HSP–27 was facilitated in cells lacking PARP-1. Thermosensitivity, however, was higher in PARP-1−/− than in PARP-1+/+ cells. Accordingly, we report that heat-shocked PARP-1 null fibroblasts showed an increased activation of proapoptotic JNK and decreased transcriptional efficiency of prosurvival NF-κB compared with wild-type counterparts. The data indicate that poly(ADP-ribosyl)ation finely regulates HSF-1 activity, and emphasize the complex role of PARP-1 in the heat-shock response of mammalian cells.

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Identification of heat-inducible long noncoding RNA MALAT1-containing novel nuclear (HiNoCo) body

Journal of Cell Science ◽

10.1242/jcs.253559 ◽

2021 ◽

Author(s):

Rena Onoguchi-Mizutani ◽

Yoshitaka Kirikae ◽

Yoko Ogura ◽

Tony Gutschner ◽

Sven Diederichs ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Response ◽

Long Noncoding Rna ◽

Mammalian Cells ◽

Noncoding Rna ◽

Heat Shock Factor ◽

Nuclear Bodies ◽

Cajal Body ◽

Heat Shock Factor 1 ◽

Shock Response

The heat shock response is critical for the survival of all organisms. Metastasis-associated long adenocarcinoma transcript 1 (MALAT1) is a long noncoding RNA localized in nuclear speckles, but its physiological role remains elusive. Here, we show that heat shock induces translocation of MALAT1 to a distinct nuclear body named heat shock-inducible noncoding RNA-containing nuclear (HiNoCo) body in mammalian cells. The MALAT1 knockout A549 cells showed reduced proliferation after heat shock. The HiNoCo body, formed by a nearby nuclear speckle, is distinct from any other known nuclear bodies, including the nuclear stress body, Cajal body, germs, paraspeckles, nucleoli, and promyelocytic leukemia body. The formation of HiNoCo body is reversible and independent of heat shock factor 1, the master transcription regulator of the heat shock response. Our results suggest the HiNoCo body participates in heat shock factor 1-independent heat shock responses in mammalian cells.

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ATF1 Modulates the Heat Shock Response by Regulating the Stress-Inducible Heat Shock Factor 1 Transcription Complex

Molecular and Cellular Biology ◽

10.1128/mcb.00754-14 ◽

2014 ◽

Vol 35 (1) ◽

pp. 11-25 ◽

Cited By ~ 28

Author(s):

Ryosuke Takii ◽

Mitsuaki Fujimoto ◽

Ke Tan ◽

Eiichi Takaki ◽

Naoki Hayashida ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Response ◽

Mammalian Cells ◽

Target Genes ◽

Acute Stress ◽

Heat Shock Factor ◽

Metabolic Adaptation ◽

Heat Shock Factor 1 ◽

Creb Binding Protein ◽

Shock Response

The heat shock response is an evolutionally conserved adaptive response to high temperatures that controls proteostasis capacity and is regulated mainly by an ancient heat shock factor (HSF). However, the regulation of target genes by the stress-inducible HSF1 transcription complex has not yet been examined in detail in mammalian cells. In the present study, we demonstrated that HSF1 interacted with members of the ATF1/CREB family involved in metabolic homeostasis and recruited them on theHSP70promoter in response to heat shock. The HSF1 transcription complex, including the chromatin-remodeling factor BRG1 and lysine acetyltransferases p300 and CREB-binding protein (CBP), was formed in a manner that was dependent on the phosphorylation of ATF1. ATF1-BRG1 promoted the establishment of an active chromatin state andHSP70expression during heat shock, whereas ATF1-p300/CBP accelerated the shutdown of HSF1 DNA-binding activity during recovery from acute stress, possibly through the acetylation of HSF1. Furthermore, ATF1 markedly affected the resistance to heat shock. These results revealed the unanticipated complexity of the primitive heat shock response mechanism, which is connected to metabolic adaptation.

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Heat shock factor 1 induces crystallin-αB to protect against cisplatin nephrotoxicity

AJP Renal Physiology ◽

10.1152/ajprenal.00201.2016 ◽

2016 ◽

Vol 311 (1) ◽

pp. F94-F102 ◽

Cited By ~ 5

Author(s):

Qiang Lou ◽

Yanzhong Hu ◽

Yuanfang Ma ◽

Zheng Dong

Keyword(s):

Heat Shock ◽

Heat Shock Response ◽

Heat Shock Factor ◽

Renal Tubular Cell ◽

Heat Shock Factor 1 ◽

Cytochrome C Release ◽

Tubular Cells ◽

Cisplatin Nephrotoxicity ◽

Shock Response ◽

Induced Apoptosis

Cisplatin, a wildly used chemotherapy drug, induces nephrotoxicity that is characterized by renal tubular cell apoptosis. In response to toxicity, tubular cells can activate cytoprotective mechanisms, such as the heat shock response. However, the role and regulation of the heat shock response in cisplatin-induced nephrotoxicity remain largely unclear. In the present study, we demonstrated the induction of heat shock factor (Hsf)1 and the small heat shock protein crystallin-αB (CryAB) during cisplatin nephrotoxicity in mice. Consistently, cisplatin induced Hsf1 and CryAB in a cultured renal proximal tubular cells (RPTCs). RPTCs underwent apoptosis during cisplatin treatment, which was increased when Hsf1 was knocked down. Transfection or restoration of Hsf1 into Hsf1 knockdown cells suppressed cisplatin-induced apoptosis, further supporting a cytoprotective role of Hsf1 and its associated heat shock response. Moreover, Hsf1 knockdown increased Bax translocation to mitochondria and cytochrome c release into the cytosol. In RPTCs, Hsf1 knockdown led to a specific downregulation of CryAB. Transfection of CryAB into Hsf1 knockdown cells diminished their sensitivity to cisplatin-induced apoptosis, suggesting that CryAB may be a key mediator of the cytoprotective effect of Hsf1. Taken together, these results demonstrate a heat shock response in cisplatin nephrotoxicity that is mediated by Hsf1 and CryAB to protect tubular cells against apoptosis.

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Protein level variability determines phenotypic heterogeneity in proteotoxic stress response

10.1101/646653 ◽

2019 ◽

Author(s):

Marie Guilbert ◽

François Anquez ◽

Alexandra Pruvost ◽

Quentin Thommen ◽

Emmanuel Courtade

Keyword(s):

Stress Response ◽

Heat Shock ◽

Heat Shock Response ◽

Phenotypic Variability ◽

Heat Shock Factor ◽

Phenotypic Heterogeneity ◽

Expression Level ◽

Heat Shock Factor 1 ◽

Response Network ◽

Shock Response

AbstractCell-to-cell variability in stress response is a bottleneck for the construction of accurate and predictive models that could guide clinical diagnosis and treatment of diseases as for instance cancers. Indeed such phenotypic heterogeneity can lead to fractional killing and persistence of a subpopulation of cells resistant to a given treatment. The heat shock response network plays a major role in protecting the proteome against several types of injuries. We combine high-throughput measurements and mathematical modeling to unveil the molecular origin of the phenotypic variability in the heat shock response network. Although the mean response coincides with known biochemical measurements, we found a surprisingly broad diversity in single cell dynamics with a continuum of response amplitudes and temporal shapes for several stimuli strengths. We theoretically predict that the broad phenotypic heterogeneity is due to network ultrasensitivity together with variations in the expression level of chaperons controlled by heat shock factor 1. We experimentally confirm this prediction by mapping the response amplitude to concentrations chaperons and heat shock factor 1 expression level.

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