&amp;cestchinlong;Activation of the mitogen-activated protein kinase pathways by heat shock

Dorion, Sonia; Landry, Jacques

doi:10.1379/1466-1268(2002)007<0200:aotmap>2.0.co;2

Cited by 86 publications

(83 citation statements)

References 66 publications

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“…However, survival kinase pathways such as PI3K-Akt, MEK1/2-ERK1/2, and the p38 MAPK pathways are activated by ischemic preconditioning (26) and are also regulating heat shock proteins and phosphorylation of Hsp27 (18). The MAPK pathway is activated by many stimulatory agents and phosphorylates downstream signaling molecules (16).…”

Section: Discussionmentioning

confidence: 99%

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Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Ali²,

Currie³

2008

American Journal of Physiology-Heart and Circulatory Physiology

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Section: Discussionmentioning

confidence: 99%

“…These survival kinases, and particularly PI3K-Akt and the MEK1/2-ERK1/2 pathways, are activated in ischemic preconditioning and ischemic postconditioning (26), and they regulate phosphorylation of Hsp27 (18). Interestingly, insulin activates MAPK (41,54,55), and MAPK activation leads to Hsp27 phosphorylation (1,63).…”

mentioning

confidence: 99%

Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Ali²,

Currie³

2008

American Journal of Physiology-Heart and Circulatory Physiology

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“…Recently, Chang et al (69) showed that the ubiquitination of c-FLIP L is regulated by JNK1-mediated activation of the ubiquitin ligase Itch. Hyperthermia is known to trigger several signaling pathways (82), and because the c-FLIP depletion upon hyperthermia treatment is very rapid, it will be important to examine whether c-FLIP S is regulated by similar kinds of signaling mechanisms as the one suggested for c-FLIP L .…”

Section: Discussionmentioning

confidence: 99%

Fever-Like Hyperthermia Controls T Lymphocyte Persistence by Inducing Degradation of Cellular FLIPshort

Meinander

Söderström

Kaunisto

et al. 2007

The Journal of Immunology

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Fever has a major impact on immune responses by modulating survival, proliferation, and endurance of lymphocytes. Lymphocyte persistence in turn is determined by the equilibrium between death and survival-promoting factors that regulate death receptor signaling in these cells. A potential integrator of death receptor signaling is the caspase-8 inhibitor c-FLIP, the expression of which is dynamically regulated, either rapidly induced or down-regulated. In this study, we show in activated primary human T lymphocytes that hyperthermia corresponding to fever triggered down-regulation of both c-FLIP-splicing variants, c-FLIPshort (c-FLIPS) and c-FLIPlong, with consequent sensitization to apoptosis mediated by CD95 (Fas/APO-1). The c-FLIP down-regulation and subsequent sensitization was specific for hyperthermic stress. Additionally, we show that the hyperthermia-mediated down-regulation was due to increased ubiquitination and proteasomal degradation of c-FLIPS, the stability of which we have shown to be regulated by its C-terminal splicing tail. Furthermore, the induced sensitivity to CD95 ligation was independent of heat shock protein 70, as thermotolerant cells, expressing substantially elevated levels of heat shock protein 70, were not rescued from the effect of hyperthermia-mediated c-FLIP down-regulation. Our findings indicate that fever significantly influences the rate of lymphocyte elimination through depletion of c-FLIPS. Such a general regulatory mechanism for lymphocyte removal has broad ramifications for fever-mediated regulation of immune responses.

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“…Sensitization of Ask1 activation by cell transformation can be a general mechanism of sensitization to apoptosis induced by a variety of agents or conditions. In addition to cisplatin and other DNA damaging agents, Ask1 can be activated by a number of agonists and toxic agents and may in fact constitute an integrator on which several signalling pathways converge to activate the stress-activated protein kinases JNK and p38 [51,52]. Several distinct regulators of Ask1 activity have been described, each mediating activation from distinct stimuli.…”

Section: Discussionmentioning

confidence: 99%

c-Myc potentiates the mitochondrial pathway of apoptosis by acting upstream of apoptosis signal-regulating kinase 1 (Ask1) in the p38 signalling cascade

Desbiens

Deschesnes

Labrie

et al. 2003

Biochemical Journal

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Cell transformation by growth-promoting oncoproteins renders cells extremely sensitive to apoptosis through an unknown mechanism affecting the mitochondrial pathway of apoptosis. We have shown previously that sensitization to apoptosis also correlated with the activation of the stress-activated protein kinase p38. In the present study, we investigated the role of p38 in c-Myc-dependent apoptosis induced by the anticancer agent cisplatin. Cisplatin treatment of Rat1 cells with deregulated expression of c-Myc resulted in nuclear fragmentation that was accompanied in all cells by the activation of Bax and the translocation of cytochrome c from the mitochondria to the cytoplasm. None of these features of apoptosis was induced in control Rat-1 cells. p38 was also activated by cisplatin only in cells with deregulated expression of c-Myc, but, in contrast with all features of apoptosis, this activation was not affected by Bcl-2. Remarkably, overexpression of an interfering mutant of the p38α isoform, but not p38β, blocked cisplatin-induced Bax activation or cytochrome c release and nuclear fragmentation. Analysis of the kinase cascade upstream of p38 revealed a c-Myc-dependent activation by cisplatin of mitogen-activated protein kinase kinase (MKK) 3/6 and apoptosis signal-regulating kinase 1 (Ask1). Inhibition of Ask1 blocked p38 activation by cisplatin and all features of apoptosis. Several of these data were confirmed using other DNA-damaging agents. The findings indicated that c-Myc potentiation of the mitochondrial pathway of apoptosis results, at least in part, from a sensitization of Ask1 activation, allowing DNA-damaging agents to induce in cascade Ask1, p38α and Bax.

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&cestchinlong;Activation of the mitogen-activated protein kinase pathways by heat shock

Cited by 86 publications

References 66 publications

Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Fever-Like Hyperthermia Controls T Lymphocyte Persistence by Inducing Degradation of Cellular FLIPshort

c-Myc potentiates the mitochondrial pathway of apoptosis by acting upstream of apoptosis signal-regulating kinase 1 (Ask1) in the p38 signalling cascade

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