INT270809

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Context Info
Confidence 0.69
First Reported 2009
Last Reported 2009
Negated 1
Speculated 0
Reported most in Body
Documents 1
Total Number 19
Disease Relevance 0.59
Pain Relevance 0.55

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

transport (Panx1) endoplasmic reticulum (Panx1) plasma membrane (Panx1)
protein complex (Panx1) cell-cell signaling (Panx1)
Anatomy Link Frequency
oocytes 5
reticulum 2
neuronal 1
macrophage 1
Panx1 (Mus musculus)
Pain Link Frequency Relevance Heat
addiction 38 93.52 High High
Inflammation 190 80.40 Quite High
cytokine 171 79.36 Quite High
Inflammatory stimuli 38 77.08 Quite High
antagonist 57 5.00 Very Low Very Low Very Low
agonist 38 5.00 Very Low Very Low Very Low
Neuropathic pain 19 5.00 Very Low Very Low Very Low
adenocard 19 5.00 Very Low Very Low Very Low
rheumatoid arthritis 19 5.00 Very Low Very Low Very Low
Potency 19 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
INFLAMMATION 228 80.40 Quite High
Apoptosis 19 76.56 Quite High
Disease 19 5.00 Very Low Very Low Very Low
Neuropathic Pain 19 5.00 Very Low Very Low Very Low
Toxicity 19 5.00 Very Low Very Low Very Low
Pressure And Volume Under Development 19 5.00 Very Low Very Low Very Low
Rheumatoid Arthritis 19 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
But, although CBX and 10panx1 inhibitory peptide completely block the membrane current recorded when panx1 is ectopically expressed (in the absence of P2X7R), they have no effect or slightly enhance the membrane current activated by P2X7R stimulation in cells expressing both panx1 and P2X7R [40]. (4) It remains unclear whether endogenous panx1 is a plasma membrane protein or an endoplasmic reticulum (ER) membrane protein or both.
Gene_expression (expressed) of panx1 in reticulum
1) Confidence 0.69 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0.04
as well as enhances the expression and activity of P2X7R and panx1.
Gene_expression (expression) of panx1
2) Confidence 0.69 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.05 Pain Relevance 0
In situ hybridization and immunohistochemistry at both light and electron microscopy levels show that panx1 is widely expressed, particularly in immune cells, endothelia, and epithelia; panx2 is relatively neuronal-specific, while panx3 shows fairly localized expression to joints and skin [45, 46, 48].
Gene_expression (expressed) of panx1 in neuronal
3) Confidence 0.69 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
But, although CBX and 10panx1 inhibitory peptide completely block the membrane current recorded when panx1 is ectopically expressed (in the absence of P2X7R), they have no effect or slightly enhance the membrane current activated by P2X7R stimulation in cells expressing both panx1 and P2X7R [40]. (4) It remains unclear whether endogenous panx1 is a plasma membrane protein or an endoplasmic reticulum (ER) membrane protein or both.
Gene_expression (expressing) of panx1 in reticulum
4) Confidence 0.69 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0.04
While this hypothesis cannot yet be ruled out in the specific case of P2X7R function, it quickly became apparent that this cannot be a general mechanism by which panx1 signals to inflammasome activation when it was found that panx1 inhibition (via CBX, panx1 gene silencing, and 10panx1 inhibitory peptide) also inhibits processing and release of bioactive IL-1?
Neg (inhibition) Gene_expression (inhibition) of panx1
5) Confidence 0.60 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
While this hypothesis cannot yet be ruled out in the specific case of P2X7R function, it quickly became apparent that this cannot be a general mechanism by which panx1 signals to inflammasome activation when it was found that panx1 inhibition (via CBX, panx1 gene silencing, and 10panx1 inhibitory peptide) also inhibits processing and release of bioactive IL-1?
Gene_expression (silencing) of panx1
6) Confidence 0.60 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
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].
Gene_expression (expected) of panx1
7) Confidence 0.60 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.05 Pain Relevance 0
However, this hypothesis also cannot be a generalized mechanism for panx1 involvement in caspase-1-dependent IL-1?
Gene_expression (involvement) of panx1
8) Confidence 0.60 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.08 Pain Relevance 0.08
Panx1 appears to be a critical component not only in P2X7R-mediated IL-1?
Gene_expression (appears) of Panx1
9) Confidence 0.60 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.15 Pain Relevance 0.11
Initial studies in which panx1 was over-expressed in oocytes suggested panx1 could act to form gap junctions in a manner similar to that known for connexins [45, 48], but no gap junction formation has been observed when panx1 is expressed in mammalian cells [40, 49] and the current understanding is that panx1 does not form gap junctions [49, 50].
Gene_expression (expressed) of panx1 in oocytes
10) Confidence 0.54 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
We have consistently failed to record large conductance single channels from panx1-expressing, or P2X7R/panx1 over-expressed, mammalian cells; there is one report of large conductance single channels (>200 pS) being observed in oocytes over-expressing panx1 [50], but this does not appear to be a consistent observation. (2) Site-directed mutagenesis of residues within the panx1 protein that result in altered voltage dependence, ion permeability, and/or unitary conductance are required to provide direct demonstration that panx1 is, itself, an ion channel. (3) If a large conductance pannexin channel is activated by P2X7R stimulation, then one would expect considerable current inhibition in the ATP-induced current in response to P2X7R stimulation.
Gene_expression (expressed) of panx1-expressing in oocytes associated with addiction
11) Confidence 0.54 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0.04
We have consistently failed to record large conductance single channels from panx1-expressing, or P2X7R/panx1 over-expressed, mammalian cells; there is one report of large conductance single channels (>200 pS) being observed in oocytes over-expressing panx1 [50], but this does not appear to be a consistent observation. (2) Site-directed mutagenesis of residues within the panx1 protein that result in altered voltage dependence, ion permeability, and/or unitary conductance are required to provide direct demonstration that panx1 is, itself, an ion channel. (3) If a large conductance pannexin channel is activated by P2X7R stimulation, then one would expect considerable current inhibition in the ATP-induced current in response to P2X7R stimulation.
Gene_expression (expressed) of panx1 in oocytes associated with addiction
12) Confidence 0.54 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0.04
This strong correlation led to the initial hypothesis that opening of dye-permeable panx1 hemichannels via P2X7R activation directly leads to inflammasome assembly and activation [40].
Gene_expression (activation) of panx1
13) Confidence 0.52 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.06 Pain Relevance 0.05
While this hypothesis cannot yet be ruled out in the specific case of P2X7R function, it quickly became apparent that this cannot be a general mechanism by which panx1 signals to inflammasome activation when it was found that panx1 inhibition (via CBX, panx1 gene silencing, and 10panx1 inhibitory peptide) also inhibits processing and release of bioactive IL-1?
Gene_expression (peptide) of 10panx1
14) Confidence 0.52 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
How might panx1 signal to activate the NLRP3 inflammasome in response to P2X7R stimulation, or to dye uptake independent stimuli?
Gene_expression (signal) of panx1
15) Confidence 0.52 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.08 Pain Relevance 0
When panx1 is ectopically expressed in HEK 293 cells lacking P2X7R, a low level of constitutive dye uptake occurs which is not otherwise observed in untransfected or vector-transfected cells nor in P2X7R-expressing cells in the absence of ATP [40].
Gene_expression (expressed) of panx1
16) Confidence 0.47 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
There are no reports of membrane currents recorded from monocytes or macrophage (or any neuronal or non-neuronal cell) having properties similar to those observed when panx1 is over-expressed in HEK 293 or other mammalian cells.
Gene_expression (expressed) of panx1 in macrophage
17) Confidence 0.47 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0.13 Pain Relevance 0.10
Initial studies in which panx1 was over-expressed in oocytes suggested panx1 could act to form gap junctions in a manner similar to that known for connexins [45, 48], but no gap junction formation has been observed when panx1 is expressed in mammalian cells [40, 49] and the current understanding is that panx1 does not form gap junctions [49, 50].
Gene_expression (expressed) of panx1 in oocytes
18) Confidence 0.47 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0
We have consistently failed to record large conductance single channels from panx1-expressing, or P2X7R/panx1 over-expressed, mammalian cells; there is one report of large conductance single channels (>200 pS) being observed in oocytes over-expressing panx1 [50], but this does not appear to be a consistent observation. (2) Site-directed mutagenesis of residues within the panx1 protein that result in altered voltage dependence, ion permeability, and/or unitary conductance are required to provide direct demonstration that panx1 is, itself, an ion channel. (3) If a large conductance pannexin channel is activated by P2X7R stimulation, then one would expect considerable current inhibition in the ATP-induced current in response to P2X7R stimulation.
Gene_expression (expressing) of panx1 in oocytes associated with addiction
19) Confidence 0.47 Published 2009 Journal Purinergic Signal Section Body Doc Link PMC2686830 Disease Relevance 0 Pain Relevance 0.05

General Comments

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