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Context Info
Confidence 0.43
First Reported 2004
Last Reported 2010
Negated 0
Speculated 0
Reported most in Abstract
Documents 3
Total Number 3
Disease Relevance 0.31
Pain Relevance 0.52

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

cytosol (Trpv1) plasma membrane (Trpv1) lipid metabolic process (Trpv1)
Anatomy Link Frequency
primary sensory neurons 2
dorsal root ganglia 2
Trpv1 (Rattus norvegicus)
Trpv1 - S116A (1)
Pain Link Frequency Relevance Heat
qutenza 6 97.48 Very High Very High Very High
Root ganglion neuron 1 90.94 High High
agonist 1 87.16 High High
Cannabinoid 2 75.00 Quite High
adenocard 1 62.28 Quite High
Hyperalgesia 1 57.36 Quite High
Inflammation 1 56.64 Quite High
nociceptor 2 54.76 Quite High
Endocannabinoid 5 50.00 Quite Low
nud 2 50.00 Quite Low
Disease Link Frequency Relevance Heat
Ganglion Cysts 1 90.78 High High
Hyperalgesia 1 57.36 Quite High
INFLAMMATION 1 56.64 Quite High
Dyspepsia 2 52.40 Quite High
Stress 2 51.20 Quite High
Gastrointestinal Disease 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In contrast, treatment of control DRGs in vitro with the CB1 receptor agonist WIN 55,212-2 decreased the levels of TRPV1 and TRPV1 phosphorylation.
Negative_regulation (decreased) of Phosphorylation (phosphorylation) of TRPV1
1) Confidence 0.43 Published 2009 Journal Gut Section Body Doc Link 18936104 Disease Relevance 0.10 Pain Relevance 0
These findings suggest that activation of the CB1 receptor can reduce the activity of TRPV1 in primary sensory neurons, and that this inhibitory effect could be mediated through the reduction of PKA-mediated phosphorylation of TRPV1.
Negative_regulation (reduction) of Phosphorylation (phosphorylation) of TRPV1 in primary sensory neurons
2) Confidence 0.43 Published 2010 Journal Acta Physiol Hung Section Abstract Doc Link 20511124 Disease Relevance 0.11 Pain Relevance 0.29
In support of this hypothesis, we found the following. 1) Overexpression of PKCmu enhanced the response of rVR1 to capsaicin and low pH, and expression of a dominant negative variant of PKCmu reduced the response of rVR1. 2) Reduction of endogenous PKCmu using antisense oligonucleotides decreased the response of exogenous rVR1 expressed in CHO cells as well as of endogenous rVR1 in dorsal root ganglion neurons. 3) PKCmu localized to the plasma membrane when overexpressed in CHO/rVR1 cells. 4) PKCmu directly bound to rVR1 expressed in CHO cells as well as to endogenous rVR1 in dorsal root ganglia or to an N-terminal fragment of rVR1, indicating a direct interaction between PKCmu and rVR1. 5) PKCmu directly phosphorylated rVR1 or a longer N-terminal fragment (amino acids 1-118) of rVR1 but not a shorter one (amino acids 1-99). 6) Mutation of S116A in rVR1 blocked both the phosphorylation of rVR1 by PKCmu and the enhancement by PKCmu of the rVR1 response to capsaicin.
Negative_regulation (blocked) of Phosphorylation (phosphorylation) of rVR1 (S116A) in dorsal root ganglia associated with ganglion cysts, qutenza and root ganglion neuron
3) Confidence 0.18 Published 2004 Journal J. Biol. Chem. Section Abstract Doc Link 15471852 Disease Relevance 0.09 Pain Relevance 0.23

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