Enhanced heat shock protein 70 expression alters proteasomal degradation of IκB kinase in experimental acute respiratory distress syndrome*

Weiss, Yoram; Bromberg, Zohar; Raj, Nichelle; Raphael, Jacob; Goloubinoff, Pierre; Ben‐Neriah, Yinon; Deutschman, Clifford S.

doi:10.1097/01.ccm.0000278915.78030.74

Cited by 102 publications

(120 citation statements)

References 59 publications

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“…Hsp70 can directly stimulate anti-inflammatory cytokines due to an inhibition of the NF-κB pathway (Schell et al 2005;Weiss et al 2007). This inhibition reduces the expression of pro-inflammatory cytokines regulated by NF-κB, such as TNF-α, IL-6, or IL-1β (De et al 2000;Pockley et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Rodriguez‐Miguelez

Fernandez‐Gonzalo

Almar

et al. 2014

AGE

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This study assessed the effects of a resistance exercise training program on the inflammatory response associated with Toll-like receptor (TLR) 2 and TLR4 signaling pathways in senior participants. Twenty-six healthy subjects (age, 69.5±1.3) were randomized to a training (TG; n=16) or a control (CG; n=10) group. TG performed an 8-week resistance training program, while CG followed their daily routines. Peripheral blood mononuclear cells were isolated from blood samples obtained before and after the intervention, and levels of proteins involved in the TLR2, TLR4, and myeloid differentiation primary response gene 88 (MyD88)-dependent and MyD88-independent pathways were analyzed. The inflammatory status was evaluated through messenger RNA (mRNA) and protein content of interleukin (IL)-10 and tumor necrosis factor alpha (TNF-α) and plasma levels of C-reactive protein (CRP). After the 8-week resistance training, TLR2 and TLR4 protein expression was reduced in TG. MyD88, p65, phosphop38, TIR domain-containing adaptor inducing interferon (TRIF), IKKi/IKKε, phospho-interferon regulatory factor (IRF) 3, and phosho-IRF7 were also downregulated in TG after the intervention. The training program induced an increase of phospho-extracellular signal-regulated kinases 1 and 2 (ERK1/2) and Hsp70 and a reduction of Hsp60. While TNF-α mRNA and protein values remained unchanged in both TG and CG, IL-10 mRNA and protein content were upregulated in TG after the intervention. CRP values decreased in TG only. The increase in Hsp70 negatively correlated with TLR2 and TLR4 downregulation. These data suggest that resistance exercise may represent an effective tool to ameliorate the pro-inflammatory status of old participants through an attenuation of MyD88-dependent and MyD88-independent TLR2 and TLR4 signaling pathways.

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Section: Discussionmentioning

confidence: 99%

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Rodriguez‐Miguelez

Fernandez‐Gonzalo

Almar

et al. 2014

AGE

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“…Noticeably, proteomic analysis showed that in the cytoplasm and the endoplasmic reticulum of human cells, the Hsp70s are respectively 7-and 14-fold more abundant than the Hsp110s (3). Thus, despite their low affinity, most of the Hsp110 molecules are expected to form loose but potent disaggregating heterocomplexes with Hsp70, leaving the remaining excess Hsp70 molecules free to carry Hsp70-specific functions, such as the catalytic unfolding of amenable misfolded monomers (12) and the pulling apart of native clathrin cages (32) or of active IB complexes (58), the activation of steroid hormone receptors, the inhibition of the heat shock transcription factor (59), or mediating proteasomal and lysosomal degradation (60).…”

Section: Discussionmentioning

confidence: 99%

Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates

Mattoo

Sharma

Priya

et al. 2013

Journal of Biological Chemistry

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142

168

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Background: Hsp110s are considered as mere nucleotide exchange factors of the Hsp70s. Results: Human cytosolic Hsp110s can use ATP to unfold misfolded polypeptides and act as equal partner with Hsp70 to solubilize stable protein aggregates. Conclusion: Hsp110s are Hsp70-like polypeptide unfolding chaperones. Significance: Hsp110s are powerful disaggregating chaperones that can collaborate with Hsp70s to detoxify misfolding proteins in degenerative diseases.

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“…This is in agreement with previous observations that the constitutive overexpression of Hsp17.7 in carrot (Daucus carota; Malik et al, 1999) or of Hsp25.3-P (Härndahl et al, 1999) and Hsp101 in Arabidopsis (Queitsch et al, 2000) provide some degree of acquired thermotolerance without heat priming. In animals too, the activities of Hsp chaperones (e.g., Hsp70 and sHsps), can block PCD by inhibiting caspase activation and IkB activity (Beere, 2004;Weiss et al, 2007). It is not unlikely that as in animal cells, the upregulation of specific Hsp chaperones in plant cells in response to heat priming, hormones, or drugs (Saidi et al, 2007;Finka et al, 2011), could inhibit the signaling for heat-induced PCD.…”

Section: Acquired Thermotolerance and Apoptosismentioning

confidence: 99%

Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance

et al. 2012

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Typically at dawn on a hot summer day, land plants need precise molecular thermometers to sense harmless increments in the ambient temperature to induce a timely heat shock response (HSR) and accumulate protective heat shock proteins in anticipation of harmful temperatures at mid-day. Here, we found that the cyclic nucleotide gated calcium channel (CNGC) CNGCb gene from Physcomitrella patens and its Arabidopsis thaliana ortholog CNGC2, encode a component of cyclic nucleotide gated Ca 2+ channels that act as the primary thermosensors of land plant cells. Disruption of CNGCb or CNGC2 produced a hyper-thermosensitive phenotype, giving rise to an HSR and acquired thermotolerance at significantly milder heat-priming treatments than in wild-type plants. In an aequorin-expressing moss, CNGCb loss-of-function caused a hyperthermoresponsive Ca 2+ influx and altered Ca 2+ signaling. Patch clamp recordings on moss protoplasts showed the presence of three distinct thermoresponsive Ca 2+ channels in wild-type cells. Deletion of CNGCb led to a total absence of one and increased the open probability of the remaining two thermoresponsive Ca 2+ channels. Thus, CNGC2 and CNGCb are expected to form heteromeric Ca 2+ channels with other related CNGCs. These channels in the plasma membrane respond to increments in the ambient temperature by triggering an optimal HSR, leading to the onset of plant acquired thermotolerance.

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Enhanced heat shock protein 70 expression alters proteasomal degradation of IκB kinase in experimental acute respiratory distress syndrome*

Cited by 102 publications

References 59 publications

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects

Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates

Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance

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