INT145680

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Context Info
Confidence 0.61
First Reported 2006
Last Reported 2009
Negated 2
Speculated 2
Reported most in Body
Documents 22
Total Number 24
Disease Relevance 11.92
Pain Relevance 5.42

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

transport (P2rx7) cell morphogenesis (P2rx7) mitochondrion organization (P2rx7)
protein complex (P2rx7) transmembrane transport (P2rx7) cytoplasm (P2rx7)
Anatomy Link Frequency
macrophages 2
granulocyte 1
vasculature 1
pore 1
lung 1
P2rx7 (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 690 99.72 Very High Very High Very High
Inflammation 715 99.60 Very High Very High Very High
tolerance 6 98.80 Very High Very High Very High
Pain 95 96.28 Very High Very High Very High
Arthritis 34 96.00 Very High Very High Very High
Neuropathic pain 38 95.88 Very High Very High Very High
Inflammatory response 87 94.80 High High
antagonist 285 94.56 High High
c fibre 8 91.84 High High
bradykinin 4 90.64 High High
Disease Link Frequency Relevance Heat
INFLAMMATION 854 99.60 Very High Very High Very High
Disease 215 99.08 Very High Very High Very High
Death 162 98.64 Very High Very High Very High
Pulmonary Disease 14 98.32 Very High Very High Very High
Stress 23 97.04 Very High Very High Very High
Asthma 19 96.64 Very High Very High Very High
Hypersensitivity 37 96.44 Very High Very High Very High
Pain 95 96.28 Very High Very High Very High
Arthritis 44 96.00 Very High Very High Very High
Neuropathic Pain 67 95.88 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
[45], whilst sensitising the P2X7R on macrophages to the cytotoxic effects of ATP [46], future studies may show that the P2X7R could be regulated by a range of ligands.
Regulation (regulated) of P2X7R in macrophages
1) Confidence 0.61 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1838907 Disease Relevance 0.63 Pain Relevance 0.24
These authors went on to examine the response of the P2X7 ????
Spec (examine) Regulation (response) of P2X7
2) Confidence 0.53 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096758 Disease Relevance 0.45 Pain Relevance 0.20
One molecule that may be involved in controlling P2X7 activity is regeneration and tolerance factor (RTF; Derks and Beaman [22]).
Regulation (controlling) of P2X7 associated with tolerance
3) Confidence 0.53 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096758 Disease Relevance 0.38 Pain Relevance 0.15
Initially, panx1 was expected to be a conduit for the high K+ efflux subsequent to P2X7R activation, but inhibition of panx1 using 10panx1 inhibitory peptide abolished caspase-1 activation without altering P2X7R-mediated K+ efflux [40].
Neg (without) Regulation (altering) of P2X7R-mediated
4) Confidence 0.42 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
The effect of P2X7 deletion on the behavioural phenotype of the mice was demonstrated in models of both inflammatory and neuropathic pain.
Regulation (effect) of P2X7 associated with inflammation and neuropathic pain
5) Confidence 0.39 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096758 Disease Relevance 0.74 Pain Relevance 0.37
Interestingly, the ability of monocytes and monocyte-like cells to demonstrate this pore activity is influenced by conditions under which these cells are cultured, suggesting that functional output of the P2X7 receptor can be regulated [34–36].
Regulation (regulated) of P2X7 receptor in pore
6) Confidence 0.28 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096759 Disease Relevance 0 Pain Relevance 0.04
Moreover, no evidence has thus far been presented to suggest that P2X7 receptor levels and/or activity are altered in human inflammatory diseases.
Regulation (altered) of P2X7 receptor associated with inflammation and disease
7) Confidence 0.28 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096759 Disease Relevance 0.27 Pain Relevance 0.12
P2X7R regulation of granulocyte function and cell death
Regulation (regulation) of P2X7R in granulocyte associated with death
8) Confidence 0.27 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1838907 Disease Relevance 1.18 Pain Relevance 0.45
Therapies directed at influencing the P2X7R
Regulation (influencing) of P2X7R
9) Confidence 0.27 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1838907 Disease Relevance 1.15 Pain Relevance 0.45
The significance of P2X7R regulation of superoxides was underlined by the observation that P2X7R expression was up-regulated around ?
Regulation (regulation) of P2X7R
10) Confidence 0.27 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1838907 Disease Relevance 1.40 Pain Relevance 0.20
A better understanding of the basic pathophysiology of the initiation of inflammation will allow us to determine whether more specific therapies such as P2X7R regulation would prevent excessive inflammatory reactions, suppress acute inflammatory reactions and possibly augment the healing process following tissue damage [112].


4.

Spec (whether) Regulation (regulation) of P2X7R associated with inflammation
11) Confidence 0.27 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1838907 Disease Relevance 0.91 Pain Relevance 0.46
As such, drugs that block P2X7 directly, or interact with proteins that modulate P2X7 activity, may have the potential to treat a broad range of inflammatory diseases, including pain associated with inflammation.


Regulation (modulate) of P2X7 associated with pain, inflammation and disease
12) Confidence 0.27 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096758 Disease Relevance 1.03 Pain Relevance 0.55
Treatment of BV-2 cells with LPS leads to a transient increase in ivermectin-sensitive P2X4 currents, while dominant P2X7 currents remain largely unaffected.
Neg (unaffected) Regulation (unaffected) of P2X7
13) Confidence 0.24 Published 2007 Journal Neuropharmacology Section Abstract Doc Link 17675190 Disease Relevance 0.28 Pain Relevance 0.19
The importance of the P2X7R on macrophages is best understood, with the P2X7R playing an important role in the formation of MGCs and in macrophage intracellular killing of mycobacteria, such as M. tuberculosis.
Regulation (importance) of P2X7R in macrophage associated with mycobacterial infection
14) Confidence 0.23 Published 2007 Journal J Inflamm (Lond) Section Body Doc Link PMC1838907 Disease Relevance 0.79 Pain Relevance 0.14
Furthermore, an antibody generated against the P2X7 receptor blocks ATP-induced IL-1?
Regulation (generated) of P2X7 receptor
15) Confidence 0.21 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096759 Disease Relevance 0 Pain Relevance 0.11
The central role of P2X7 receptors, as co-stimulators of the posttranslational processing of IL–?
Regulation (role) of P2X7
16) Confidence 0.16 Published 2006 Journal Purinergic Signal Section Body Doc Link PMC2096753 Disease Relevance 0.08 Pain Relevance 0.04
Among various subtypes of the ionotropic P2 receptors, the role of P2X7 receptors in the microglial response is especially well delineated.
Regulation (role) of P2X7
17) Confidence 0.16 Published 2006 Journal Purinergic Signal Section Body Doc Link PMC2096753 Disease Relevance 0.13 Pain Relevance 0.06
Differential regulation of microglial P2X4 and P2X7 ATP receptors following LPS-induced activation.
Regulation (regulation) of P2X7
18) Confidence 0.16 Published 2007 Journal Neuropharmacology Section Title Doc Link 17675190 Disease Relevance 0.36 Pain Relevance 0.21
Studies in several cellular systems have provided evidence that P2 receptor modulation can affect cytokine production, and mechanistic features of this regulation have emerged.
Regulation (modulation) of P2 receptor associated with cytokine
19) Confidence 0.12 Published 2007 Journal Purinergic Signal Section Abstract Doc Link PMC2096759 Disease Relevance 0.25 Pain Relevance 0.33
ATP acting via the P2X7 receptor activates a number of intracellular kinases including members of the MAP kinase family ERK and JNK [23, 109–112], Rho effector kinases [113, 114], and the protein tyrosine kinase p56lck [115].
Regulation (acting) of P2X7 receptor
20) Confidence 0.12 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096759 Disease Relevance 0 Pain Relevance 0

General Comments

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