INT136651

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.42
First Reported 2001
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 30
Total Number 30
Disease Relevance 1.09
Pain Relevance 3.11

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

cytosol (Calm2) nucleoplasm (Calm2) cytoskeleton (Calm2)
cell cycle (Calm2) cellular_component (Calm2) biological_process (Calm2)
Anatomy Link Frequency
tail 2
neuronal 1
plasma 1
pericyte 1
Calm2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Kinase C 78 99.84 Very High Very High Very High
sodium channel 12 98.60 Very High Very High Very High
addiction 99 98.44 Very High Very High Very High
Pyramidal cell 24 95.76 Very High Very High Very High
fluoxetine 1 90.84 High High
antidepressant 1 90.40 High High
Peripheral nervous system 2 89.84 High High
local anesthetic 6 87.68 High High
analgesia 2 82.04 Quite High
tetrodotoxin 57 79.72 Quite High
Disease Link Frequency Relevance Heat
Epilepsy 16 92.16 High High
Nociception 2 91.56 High High
Status Epilepticus 57 90.72 High High
Shock 8 89.36 High High
Schizophrenia 3 87.44 High High
Channelopathies 16 71.40 Quite High
Toxicity 1 70.24 Quite High
Ganglion Cysts 158 66.80 Quite High
Apoptosis 25 50.16 Quite High
Death 2 48.88 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Inhibition of CaM binding suppresses pericyte Na(V) currents.
CaM Binding (binding) of in pericyte
1) Confidence 0.42 Published 2007 Journal Am. J. Physiol. Renal Physiol. Section Abstract Doc Link 16912065 Disease Relevance 0 Pain Relevance 0.17
However, the TFP inhibition was not replicated by whole cell dialysis of a calmodulin inhibitory peptide, indicating that major effects of TFP do not involve a disruption of CaM-channel interactions.
CaM Binding (interactions) of
2) Confidence 0.36 Published 2006 Journal J. Neurophysiol. Section Abstract Doc Link 16807347 Disease Relevance 0.08 Pain Relevance 0.76
CaM can bind to the C-termini of voltage-gated sodium channels and modulate their functional properties; therefore we investigated if TFP modulation of sodium channels was due to CaM inhibition.
CaM Binding (bind) of associated with sodium channel
3) Confidence 0.32 Published 2006 Journal J. Neurophysiol. Section Abstract Doc Link 16807347 Disease Relevance 0.09 Pain Relevance 0.54
Using pull-down assays and immunoprecipitation experiments, we verified that CaM binds to either full-length Na(V)1.3 or a GST-Na(V)1.3 COOH-terminal fusion protein.
CaM Binding (binds) of
4) Confidence 0.31 Published 2007 Journal Am. J. Physiol. Renal Physiol. Section Abstract Doc Link 16912065 Disease Relevance 0 Pain Relevance 0.33
In the case of group III mGluRs, the interaction with CaM is important in regulating the efficacy of G protein activation [27,28].
CaM Binding (interaction) of
5) Confidence 0.27 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Association of Siah1a with group I mGluRs can also prevent the interaction of CaM and the receptor [36].
CaM Binding (interaction) of
6) Confidence 0.27 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.06
Finally, CaM binding to the mGluRs did not appear to be Ca2+-dependent.
CaM Binding (binding) of
7) Confidence 0.27 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
This model predicts that Siah1a association produces its effect by disrupting the interaction of CaM with the group I mGluRs.
CaM Binding (interaction) of
8) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
CaM binding to both group I and group III mGluRs can be inhibited by serine/threonine phosphorylation at specific sites [25,28].
CaM Binding (binding) of
9) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Calmodulin (CaM), a calcium binding protein intricately involved in intracellular signaling, interacts with the C-terminal tail of group I mGluRs [25].
CaM Binding (interacts) of in tail
10) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.07
For example, group I and group III mGluRs are both known to bind Calmodulin (CaM) [25,26].
CaM Binding (bind) of
11) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.03
However, CaM can also interact with group III mGluRs [26,28].
CaM Binding (interact) of
12) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.03
Finally, coexpression of CaM reversed the effect of Siah1a on mGluR5b, indicating that the interaction of CaM and Siah1a in binding to group I mGluRs plays a novel and important role in mGluR function.


CaM Binding (interaction) of
13) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0.07 Pain Relevance 0.03
These results indicate that the presence of high levels of CaM can reverse the effect of Siah1a on calcium current modulation, presumably by competing for binding on the C-terminal tail of the receptor.
CaM Binding (binding) of in tail
14) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
The data imply two possible mechanisms for the effect of Siah1a on mGluR signaling: First, CaM association with group I mGluRs increases G protein coupling (or perhaps is required, as may be the case with group III mGluRs).
CaM Binding (association) of
15) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Recent data suggests that the association of CaM with group III mGluRs is necessary for normal G protein activation [27].
CaM Binding (association) of
16) Confidence 0.21 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
When Siah1a is caused to express heterologously (at presumably high levels) it expresses at levels high enough to out-compete native CaM for mGluR binding.
CaM Binding (binding) of
17) Confidence 0.20 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Phosphorylation of the receptors at specific sites prevents CaM binding to mGluRs [25].
CaM Binding (binding) of
18) Confidence 0.20 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.06
Alternatively, the presence of Siah1a itself may occlude G protein coupling, with the CaM interaction being incidental.
CaM Binding (interaction) of
19) Confidence 0.20 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0
Although CaM has been known to associate with group I mGluRs for some time, the functional role of this interaction is unknown.
CaM Binding (associate) of
20) Confidence 0.20 Published 2001 Journal BMC Neurosci Section Body Doc Link PMC58838 Disease Relevance 0 Pain Relevance 0.03

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox