INT215496

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Context Info
Confidence 0.44
First Reported 2007
Last Reported 2009
Negated 1
Speculated 0
Reported most in Body
Documents 10
Total Number 10
Disease Relevance 1.88
Pain Relevance 2.41

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

Golgi apparatus (P2rx3)
Anatomy Link Frequency
oocyte 2
sensory neurons 1
P2rx3 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
agonist 23 100.00 Very High Very High Very High
Kinase C 648 99.84 Very High Very High Very High
dorsal root ganglion 77 99.60 Very High Very High Very High
antagonist 3 97.04 Very High Very High Very High
Spinal cord 6 91.68 High High
Pain 44 91.60 High High
Neuropathic pain 13 89.24 High High
Brush evoked pain 19 86.44 High High
Eae 4 84.00 Quite High
Peripheral nerve injury 10 64.00 Quite High
Disease Link Frequency Relevance Heat
Ganglion Cysts 78 99.60 Very High Very High Very High
Nociception 46 94.64 High High
Hypersensitivity 9 93.24 High High
Pain 45 91.60 High High
Nervous System Injury 71 90.64 High High
Neuropathic Pain 35 89.24 High High
Injury 5 84.00 Quite High
Hepatitis 18 69.40 Quite High
INFLAMMATION 2 41.60 Quite Low
Hyperalgesia 1 21.28 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
ATP receptor agonist-dependent phosphorylation of cPLA2 and CaMKII were inhibited either by the selective P2X3R/P2X2+3R antagonist A-317491 or by the nonselective VDCC blocker cadmium.
Phosphorylation (phosphorylation) of ATP receptor associated with antagonist and agonist
1) Confidence 0.44 Published 2009 Journal Mol Pain Section Body Doc Link PMC2684092 Disease Relevance 1.20 Pain Relevance 0.92
However, phosphorylated P2X2 or P2X3 subunits could not be detected by immunoblotting with a phosphothreonine-specific antibody (Fig. 4a).
Phosphorylation (phosphorylated) of P2X3
2) Confidence 0.37 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.07
Discernible phosphorylation of P2X2 and P2X3 receptors might be obscured by a low level of endogenous PKC.
Phosphorylation (phosphorylation) of P2X3 associated with kinase c
3) Confidence 0.37 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.31
54 kDa of the P2X2 or P2X3 subunit, respectively, the presence of which could be verified by immunoblotting (right panel)

PMA or calyculin A do not enhance phosphorylation of P2X3 receptors in intact HEK cells

Phosphorylation (phosphorylation) of P2X3
4) Confidence 0.37 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0.07 Pain Relevance 0.22
Fig. 7PMA and calyculin A do not induce phosphorylation of P2X3 receptors in intact HEK cells.
Phosphorylation (phosphorylation) of P2X3
5) Confidence 0.37 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.11
Note that phosphorylation of the P2X3 receptor or the EGFP-tagged P2X2 receptor is not detectable, whereas a positive control—the EGFP-tagged splicing factor SF3B1 (migration mass 97 kDa [23])—was detected by the antibody. b The same samples as in panel a were immunoblotted using peptide-specific P2X2 and P2X3 subunit polyclonal antibodies to verify the expression of the transfected genes

PMA-activated PKC does not drive the phosphorylation of P2X2 or P2X3 receptors

Phosphorylation (phosphorylation) of P2X3 associated with kinase c
6) Confidence 0.37 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.10
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 P2X3 in sensory neurons associated with nociception, pain, kinase c, nervous system injury and hypersensitivity
7) Confidence 0.28 Published 2007 Journal Purinergic Signal Section Title Doc Link PMC2072911 Disease Relevance 0.37 Pain Relevance 0.29
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 P2X3 associated with kinase c
8) Confidence 0.28 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0.15
Fig. 3Immunoblots show no constitutive phosphorylation of oocyte-expressed P2X2 or P2X3 receptors.
Neg (no) Phosphorylation (phosphorylation) of P2X3 in oocyte
9) Confidence 0.28 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2072911 Disease Relevance 0 Pain Relevance 0
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 P2X3 in oocytes
10) Confidence 0.28 Published 2007 Journal Purinergic Signal Section Abstract Doc Link PMC2072911 Disease Relevance 0.24 Pain Relevance 0.24

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