INT228678

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Context Info
Confidence 0.78
First Reported 2008
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 15
Total Number 18
Disease Relevance 3.18
Pain Relevance 2.76

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

cytosol (Mtor) mitochondrion (Mtor) Golgi apparatus (Mtor)
endoplasmic reticulum (Mtor) nucleus (Mtor) kinase activity (Mtor)
Anatomy Link Frequency
dorsal 2
hypothalamus 2
skin 2
muscle 1
Mtor (Rattus norvegicus)
Pain Link Frequency Relevance Heat
nociceptor 205 99.60 Very High Very High Very High
Paracetamol 240 99.32 Very High Very High Very High
Calcitonin gene-related peptide 45 98.68 Very High Very High Very High
Hippocampus 100 97.48 Very High Very High Very High
long-term potentiation 36 94.72 High High
Inflammatory response 5 94.60 High High
Sciatic nerve 25 86.48 High High
Intracerebroventricular 20 86.16 High High
Pain 40 73.12 Quite High
cytokine 9 71.00 Quite High
Disease Link Frequency Relevance Heat
Tuberous Sclerosis 4 98.88 Very High Very High Very High
Obesity 165 95.00 High High
INFLAMMATION 23 94.24 High High
Aging 160 94.12 High High
Appetite Loss 56 91.08 High High
Neointima 11 86.40 High High
Starvation 2 83.28 Quite High
Anxiety Disorder 8 78.44 Quite High
Hypertrophy 4 77.44 Quite High
Pain 65 73.12 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Rapamycin is a specific inhibitor of mTOR function that prevents p70S6K and 4E-BPs phosphorylation thus interfering with the initiation of translation [11] of a subset of mRNAs rather than general translation [12].
Phosphorylation (phosphorylation) of mTOR
1) Confidence 0.78 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2695538 Disease Relevance 0 Pain Relevance 0.12
Using western blotting and immunohistochemistry, we found that intraplantar injections of rapamycin reduced phosphorylation of downstream targets of mTOR, therefore suggesting that mTOR activity was inhibited by rapamycin.
Phosphorylation (phosphorylation) of mTOR
2) Confidence 0.70 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2276314 Disease Relevance 0.09 Pain Relevance 0.08
The mTOR inhibitor rapamycin blocks the phosphorylation of 4E-BP1/2, S6K and S6 in skin
Phosphorylation (phosphorylation) of mTOR in skin
3) Confidence 0.69 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2276314 Disease Relevance 0.06 Pain Relevance 0.34
Anti-phospho-mTOR (Ser2448; used at a concentration of 1?
Phosphorylation (phospho) of mTOR
4) Confidence 0.69 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2276314 Disease Relevance 0.14 Pain Relevance 0.31
We were also able to localize phosphorylated downstream targets of mTOR (Fig. 2A) co-existing with PGP, CGRP and N52 such as phospho-4E-BP1/2, phospho-S6K and phospho-S6 protein in skin tissue, (Fig. 2D-F and Fig. 3B).
Phosphorylation (phosphorylated) of mTOR in skin associated with calcitonin gene-related peptide
5) Confidence 0.69 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2276314 Disease Relevance 0 Pain Relevance 0.44
We found that blockade of BDNF with function-blocking anti-BDNF antibodies delivered into dorsal CA1 15 min before training abolished the IA learning-induced increase in mTOR (Figure 5A) and p70S6K (Figure 5B) phosphorylation.
Phosphorylation (phosphorylation) of mTOR in dorsal
6) Confidence 0.69 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2695538 Disease Relevance 0 Pain Relevance 0.06
45 h after training hindered the IA learning-induced increase in mTOR (Figure 5C) and p70S6K (Figure 5D) phosphorylation that takes place 3 h after training.
Phosphorylation (phosphorylation) of mTOR
7) Confidence 0.68 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2695538 Disease Relevance 0 Pain Relevance 0.03
Compared to cells treated with insulin alone, cells treated with rosiglitazone before insulin stimulus demonstrated significant inhibition of phosphorylated mTOR.


Phosphorylation (phosphorylated) of mTOR
8) Confidence 0.64 Published 2008 Journal Yonsei Medical Journal Section Body Doc Link PMC2615285 Disease Relevance 0.30 Pain Relevance 0
Immunoblot analysis with an antibody that detects mTOR only when phosphorylated at serine 2448 (p-mTOR), i.e., when active, revealed two peaks of increased p-mTOR immunoreactivity in the dorsal hippocampus of trained rats sacrificed immediately (0 h) or 3 h after training (0 h: +104% respect to naïve, p<0.001, n?
Phosphorylation (phosphorylated) of mTOR in dorsal associated with hippocampus
9) Confidence 0.60 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2695538 Disease Relevance 0.08 Pain Relevance 0.14
Interestingly, these data do not appear to predict down-stream Akt signaling since the phosphorylation level of mTOR (Ser2448) [9] (Figure 2A), tuberous sclerosis complex-2 (TSC2) and forkhead box O1 (FoxO1) (data not shown) was lower in the very aged muscle.
Phosphorylation (phosphorylation) of mTOR in muscle associated with tuberous sclerosis
10) Confidence 0.53 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.43 Pain Relevance 0.07
Akt function is controlled, at least in part, by the phosphorylation of Ser473 by the mammalian target of rapamycin (mTOR) and the phosphorylation of Thr308 by phosphoinositide-dependent kinase (PDK)-1 [10]–[12].
Phosphorylation (phosphorylation) of mTOR
11) Confidence 0.53 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.58 Pain Relevance 0.04
Paradoxically, these increases in Akt phosphorylation were associated with diminished mammalian target of rapamycin (mTOR) phosphorylation, along with decreased levels of insulin receptor beta (IR-?)
Phosphorylation (phosphorylation) of mTOR
12) Confidence 0.53 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2712760 Disease Relevance 0.29 Pain Relevance 0.16
Phosphorylated mTOR together with other downstream components of the translational machinery were localized to a subset of myelinated sensory fibers in rat cutaneous tissue.
Phosphorylation (Phosphorylated) of mTOR
13) Confidence 0.47 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2276314 Disease Relevance 0.32 Pain Relevance 0.30
Furthermore, the reduction of AMPK and ACC phosphorylation and increase in phosphorylation of proteins involved in mTOR signal transduction, observed in the hypothalamus after leptin infusion, were more pronounced in both lean and diet-induced obesity rats after acute exercise.
Phosphorylation (phosphorylation) of mTOR in hypothalamus associated with obesity
14) Confidence 0.46 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2585815 Disease Relevance 0.26 Pain Relevance 0.04
Furthermore, the reduction of AMPK and ACC phosphorylation and increase in phosphorylation of proteins involved in mTOR signal transduction, observed in the hypothalamus after leptin infusion, were more pronounced in both lean and diet-induced obesity rats after acute exercise.
Phosphorylation (phosphorylation) of mTOR in hypothalamus associated with obesity
15) Confidence 0.46 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2585815 Disease Relevance 0.26 Pain Relevance 0.04
Another target molecule for the control of food intake and energy homeostasis is represented by the phosphoprotein mammalian target of rapamycin, mTOR, in which the PI(3)K/Akt pathway has been suggested to affect the mTOR phosphorylation state and catalytic activity [13].
Phosphorylation (phosphorylation) of mTOR
16) Confidence 0.46 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2585815 Disease Relevance 0.18 Pain Relevance 0
86.8%, respectively; P<0.05; Figure 2A), while chronic acetaminophen treatment restored the amount of phosphorylated and total mTOR to a level equivalent to that seen in 6- and 27-month old animals (P>0.05).
Phosphorylation (phosphorylated) of mTOR associated with paracetamol
17) Confidence 0.41 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.11 Pain Relevance 0.60
Since we did not observe modifications in the phosphorylation of JAK2 and the downstream targets of mTOR after exercise, these data suggest that the cross-talk between insulin, IL-6 and leptin have an essential role in controlling food intake after exercise.
Phosphorylation (phosphorylation) of mTOR
18) Confidence 0.40 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2585815 Disease Relevance 0.07 Pain Relevance 0

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