INT215163

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Context Info
Confidence 0.60
First Reported 2007
Last Reported 2007
Negated 1
Speculated 0
Reported most in Body
Documents 19
Total Number 19
Disease Relevance 1.43
Pain Relevance 3.62

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

plasma membrane (P2rx2)
Anatomy Link Frequency
oocyte 2
sensory neurons 1
P2rx2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 1152 100.00 Very High Very High Very High
bradykinin 33 97.80 Very High Very High Very High
substance P 37 94.44 High High
Glutamate receptor 17 91.28 High High
Pain 93 91.24 High High
Inflammatory mediators 1 85.60 High High
Inflammation 23 83.40 Quite High
Stimulus evoked pain 5 75.20 Quite High
Hyperalgesia 17 67.40 Quite High
allodynia 31 66.72 Quite High
Disease Link Frequency Relevance Heat
Nociception 99 94.28 High High
Hypersensitivity 24 92.88 High High
Pain 105 91.24 High High
Nervous System Injury 98 90.28 High High
INFLAMMATION 24 85.20 High High
Inflammatory Pain 10 74.52 Quite High
Hyperalgesia 21 67.40 Quite High
Neuropathic Pain 88 66.72 Quite High
Ganglion Cysts 44 50.00 Quite Low
Hepatitis 32 24.16 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, even when we used the same phosphothreonine-proline-specific antibody as Boue-Grabot et al. [19], we could not demonstrate phosphorylation of P2X2 receptors in our experiments (data not shown).
Phosphorylation (phosphorylation) of P2X2
1) Confidence 0.60 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.26
Further evidence against a direct PKC-mediated P2X receptor phosphorylation comes from co-expression studies of P2X1 and G protein-coupled receptors.
Phosphorylation (phosphorylation) of P2X associated with kinase c
2) Confidence 0.60 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.33
The underlying mechanism, however, is unlikely to involve direct PKC-mediated phosphorylation of P2X receptors.
Phosphorylation (phosphorylation) of P2X associated with kinase c
3) Confidence 0.60 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.27
However, phosphorylated P2X2 or P2X3 subunits could not be detected by immunoblotting with a phosphothreonine-specific antibody (Fig. 4a).
Phosphorylation (phosphorylated) of P2X2
4) Confidence 0.60 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.07
To address the possibility that P2X receptor phosphorylation is host cell specific, we analysed HEK293 cells transiently transfected with P2X2 or P2X3 expression plasmids.
Phosphorylation (phosphorylation) of P2X
5) Confidence 0.59 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.04
Discernible phosphorylation of P2X2 and P2X3 receptors might be obscured by a low level of endogenous PKC.
Phosphorylation (phosphorylation) of P2X2 associated with kinase c
6) Confidence 0.59 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.31
As apparent from Fig. 3c, neither N-terminally nor C-terminally His-tagged P2X2 receptor became phosphorylated, as evidenced by immunoblotting with a phosphor-specific anti-threonine antibody (Fig. 3c).
Phosphorylation (phosphorylated) of P2X2
7) Confidence 0.59 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.04
Boue-Grabot et al. [19] have demonstrated phosphorylation of P2X2 receptors expressed in HEK293 cells.
Phosphorylation (phosphorylation) of P2X2
8) Confidence 0.59 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.04
No phosphorylation signal could be detected at the SDS-PAGE migration position of P2X2 subunits, which were visualized by immunoblotting with the P2X2 subunit polyclonal antibody (middle panel) or PhosphorImager scanning of incorporated [35S]methionine (right panel)
Phosphorylation (phosphorylation) of P2X2
9) Confidence 0.52 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.04
The P2X2 subunit shares with other P2X subunit isoforms a conserved consensus site for PKC phosphorylation (TXR/K, where T is the phosphorylation site and X denotes any amino acid; see Fig. 1a, b).
Phosphorylation (phosphorylation) of P2X associated with kinase c
10) Confidence 0.52 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.20
Phosphorylation of the PKC sites in P2X1 and P2X2 receptor slowed the rate of inactivation of ATP currents [49,50].
Phosphorylation (Phosphorylation) of P2X2
11) Confidence 0.49 Published 2007 Journal Mol Pain Section Body Doc Link PMC2063498 Disease Relevance 0.12 Pain Relevance 0.24
Biochemically, however, we were unable to demonstrate by various experimental approaches a direct phosphorylation of wild-type P2X2 and P2X3 receptors expressed in both Xenopus laevis oocytes and HEK293 cells.
Phosphorylation (phosphorylation) of P2X2 in oocytes
12) Confidence 0.46 Published 2007 Journal Purinergic Signal Section Abstract Doc Link PMC2072911 Disease Relevance 0.24 Pain Relevance 0.24
The underlying mechanism, however, is unlikely to involve direct PKC-mediated P2X receptor phosphorylation.



Phosphorylation (phosphorylation) of P2X associated with kinase c
13) Confidence 0.46 Published 2007 Journal Purinergic Signal Section Abstract Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.17
The aim of this study was to assess biochemically the conditions in which P2X2 and P2X3 receptors become directly phosphorylated by PKC in a heterologous system.
Phosphorylation (phosphorylated) of P2X2 associated with kinase c
14) Confidence 0.46 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.15
Lack of evidence for direct phosphorylation of recombinantly expressed P2X2 and P2X3 receptors by protein kinase C

P2X3 and P2X2+3 receptors are present on sensory neurons, where they contribute not only to transient nociceptive responses, but also to hypersensitivity underlying pathological pain states elicited by nerve injuries.

Phosphorylation (phosphorylation) of P2X2 in sensory neurons associated with nociception, pain, kinase c, nervous system injury and hypersensitivity
15) Confidence 0.46 Published 2007 Journal Purinergic Signal Section Title Doc Link PMC2072911 Disease Relevance 0.37 Pain Relevance 0.29
Fig. 3Immunoblots show no constitutive phosphorylation of oocyte-expressed P2X2 or P2X3 receptors.
Neg (no) Phosphorylation (phosphorylation) of P2X2 in oocyte
16) Confidence 0.46 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0
Some of the regulation is mediated through the phosphorylation of P2X receptors by protein kinases [117, 118].
Phosphorylation (phosphorylation) of P2X
17) Confidence 0.45 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096756 Disease Relevance 0.57 Pain Relevance 0.46
It is unclear how phosphorylation of the conserved PKA site changes P2X receptor activity.
Phosphorylation (phosphorylation) of P2X
18) Confidence 0.38 Published 2007 Journal Mol Pain Section Body Doc Link PMC2063498 Disease Relevance 0.13 Pain Relevance 0.18
The existence of a proline in the P+1 position in several P2X subunit isoforms (P2X1, P2X2, P2X4) might be one causative factor preventing direct phosphorylation by PKC.
Phosphorylation (phosphorylation) of P2X2 associated with kinase c
19) Confidence 0.26 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.28

General Comments

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