INT66919

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Context Info
Confidence 0.69
First Reported 1996
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 27
Total Number 29
Disease Relevance 14.78
Pain Relevance 3.24

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

nucleolus (HSF1) nucleus (HSF1) protein complex (HSF1)
cytoplasm (HSF1)
Anatomy Link Frequency
HSF 3
band 1
body 1
HSF1 (Homo sapiens)
Pain Link Frequency Relevance Heat
cINOD 56 99.96 Very High Very High Very High
Inflammation 24 98.76 Very High Very High Very High
Osteoarthritis 6 97.96 Very High Very High Very High
rheumatoid arthritis 64 97.92 Very High Very High Very High
Inflammatory stimuli 5 94.80 High High
Arthritis 14 89.20 High High
cytokine 30 78.56 Quite High
Spinal cord 240 59.48 Quite High
Glutamate 40 5.00 Very Low Very Low Very Low
Immobilon 40 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 1446 100.00 Very High Very High Very High
INFLAMMATION 55 99.68 Very High Very High Very High
Stress 556 98.04 Very High Very High Very High
Osteoarthritis 12 97.96 Very High Very High Very High
Rheumatoid Arthritis 64 97.92 Very High Very High Very High
Targeted Disruption 100 96.84 Very High Very High Very High
Repression 4 95.52 Very High Very High Very High
Injury 40 91.56 High High
Death 139 91.12 High High
Arthritis 12 89.20 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
HSF-1 was activated in these cells by a wide range of classes of non-steroidal antiinflammatory drugs (NSAIDs) while being strongly repressed by pro-inflammatory stimuli.
Positive_regulation (activated) of HSF-1 in HSF associated with inflammation, cinod and inflammatory stimuli
1) Confidence 0.69 Published 1996 Journal Biochem. Biophys. Res. Commun. Section Abstract Doc Link 8954923 Disease Relevance 0.80 Pain Relevance 0.38
In addition, sodium salicylate and additional NSAIDs used at concentrations that activate HSF1 also inhibited the expression of other monocytic genes (TNF-alpha, IL-1beta, IL-6, IL-8, IL-10, ICAM-1) activated by exposure to a pro-inflammatory stimulus (lipopolysaccharide, LPS).
Positive_regulation (activate) of HSF1 associated with cinod and inflammatory stimuli
2) Confidence 0.68 Published 1999 Journal Cytokine Section Abstract Doc Link 10328874 Disease Relevance 0.72 Pain Relevance 0.73
Recent studies have shown that the non-steroidal anti-inflammatory drugs (NSAIDs) activate heat shock transcription factor (HSF1) from a latent cytoplasmic form to a nuclear, DNA binding state.
Positive_regulation (activate) of HSF1 associated with inflammation, shock and cinod
3) Confidence 0.68 Published 1999 Journal Cytokine Section Abstract Doc Link 10328874 Disease Relevance 0.52 Pain Relevance 0.52
The increased HSF1 contributed centrally to the cytoprotective activity of riluzole as hsf1 gene knockout negated the synergistic activity of riluzole and conditioning heat shock to confer cell survival under oxidative stress.
Positive_regulation (increased) of HSF1 associated with stress, targeted disruption and shock
4) Confidence 0.66 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2481402 Disease Relevance 0.90 Pain Relevance 0
Immuno-Western and -cytochemical analysis of HSF1 show that riluzole increased the amount of cytosolic HSF1 to afford a greater activation of HSF1 upon heat shock.
Positive_regulation (increased) of HSF1 associated with shock
5) Confidence 0.66 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2481402 Disease Relevance 0.87 Pain Relevance 0
Immuno-Western and -cytochemical analysis of HSF1 show that riluzole increased the amount of cytosolic HSF1 to afford a greater activation of HSF1 upon heat shock.
Positive_regulation (activation) of HSF1 associated with shock
6) Confidence 0.66 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2481402 Disease Relevance 0.88 Pain Relevance 0
A fundamental step in the activation of HSF1 is nuclear translocation.24,25 In the absence of stress, HSF1 is retained in the cytoplasm by inhibitory associations with Hsp70, Hsp90, and various cochaperones.(26) We demonstrated that HNE promotes the nuclear translocation of HSF1 using Western blot analysis, and showed the enhanced transcription of a luciferase reporter gene under the regulation of a conserved heat shock element.(27)
Positive_regulation (activation) of HSF1 associated with stress and shock
7) Confidence 0.59 Published 2010 Journal Accounts of Chemical Research Section Body Doc Link PMC2873822 Disease Relevance 1.00 Pain Relevance 0
These findings reflect the properties of HSF1 which can be activated to at least two DNA binding forms only one of which activates heat shock promoters and suggest that individual NSAID family members may differentially induce one or other of these forms.
Positive_regulation (activated) of HSF1 associated with shock and cinod
8) Confidence 0.49 Published 1999 Journal Cytokine Section Abstract Doc Link 10328874 Disease Relevance 0.60 Pain Relevance 0.79
There is ample literature evidence that inhibition of the UPS pathway, e.g. by the use of peptide aldehyde inhibitors including MG132, promotes the rapid activation of HSF1 [19], [20], [21].
Positive_regulation (activation) of HSF1
9) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.09 Pain Relevance 0
In this context, our observation that riluzole increased HSF1 reserve to allow for a more robust mobilization of HSF1 and induction of the HSR would suggest that riluzole and conditioning heat shock could have synergistic effect in protecting cells against stress-induced injury and death.
Positive_regulation (increased) of HSF1 associated with stress, injury, shock and death
10) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 1.19 Pain Relevance 0
We show in Fig. 2B that riluzole increased the amount of monomeric HSF1 in the cytosol of control, unstressed cells (Fig. 2B: lane 3 versus 1).
Positive_regulation (increased) of HSF1
11) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.39 Pain Relevance 0
The effect of riluzole was qualitatively different from drugs that inhibit proteasome function: riluzole gave a delayed increase in the amount but not the acute activation of HSF1.
Neg (not) Positive_regulation (activation) of HSF1
12) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.06 Pain Relevance 0
The result in Fig. 2A suggests that riluzole increased the amount of HSF1 principally in the cysotol, and this increased reserve allowed for a greater mobilization and nuclear translocation of HSF1 upon stress.
Positive_regulation (increased) of HSF1 associated with stress
13) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.27 Pain Relevance 0
M, 3 hr; lanes 5 and 6) and heat shock (42°C, 2 hr; lanes 7 and 8) that acutely promoted the activation of HSF1- as indicated by nuclear localization and hyperphosphorylation (supershift of the HSF1 band).
Positive_regulation (activation) of HSF1 in band associated with shock
14) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.30 Pain Relevance 0
In Fig. 6D, we show that the riluzole-induced increase in HSF1 drove a higher expression of the 72 kDa HSP70 protein under both control (37°C) and heat shock (42°C) conditions, with an optimal increase observed at 2 ?
Positive_regulation (increase) of HSF1 associated with shock
15) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.15 Pain Relevance 0
Treatment of the hsf+/+ cells with riluzole gave a similar increase in HSF1 (lanes 5 & 6).
Positive_regulation (increase) of HSF1
16) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.21 Pain Relevance 0
-lactone; and Ada-(ahx)3-(Leu)3-vinyl sulfone (BIOMOL Int, LP) also promoted the activation of HSF1 as determined by it's hyperphosphorylation, nuclear translocation and trimerization (data not shown).
Positive_regulation (activation) of HSF1
17) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.07 Pain Relevance 0
M, 18 hr; lanes 3 and 4) gave a significant increase in the amount of HSF1 in the cytosol and a small but reproducible increase in the nuclear fraction (Fig. 2A: cytosol, lanes 3 versus 1; nuclear, lanes 4 versus 2).
Positive_regulation (increase) of HSF1
18) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.32 Pain Relevance 0
Transfection of the cells with pCep4hHSF1 drove the expression of HSF1, and riluzole treatment increased the level of HSF1 (lane 3 & 4).
Positive_regulation (increased) of HSF1
19) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.22 Pain Relevance 0
Further, in despite the activation of HSF1, chloroquine treatment had dire consequence in cell viability–most of the cells were dying/dead after 8 hr incubation in the presence of 0.2 mM chloroquine.
Positive_regulation (activation) of HSF1
20) Confidence 0.44 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2481402 Disease Relevance 0.09 Pain Relevance 0

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