INT288597

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Context Info
Confidence 0.01
First Reported 2009
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 8
Disease Relevance 0.17
Pain Relevance 0

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

endoplasmic reticulum (CAV1, Kcnma1) plasma membrane (CAV1, Kcnma1) endosome (CAV1)
transport (Kcnma1) mitochondrion (CAV1) small molecule metabolic process (CAV1)
CAV1 (Homo sapiens)
Kcnma1 (Mus musculus)
Pain Link Frequency Relevance Heat
potassium channel 16 35.80 Quite Low
anesthesia 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 8 96.92 Very High Very High Very High
Infection 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
We stress that, in spite of the differences between the two studies, they do agree on the localization and amino acid sequence of the consensus site that mediates binding of the maxi-K channel to caveolin [8].
caveolin Binding (binding) of maxi-K channel associated with stress
1) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0.10 Pain Relevance 0
It is thus possible that changes in the association of the maxi-K channel with various caveolin isoforms plays a role in determining which other cell signaling molecules the maxi-K channel is in proximity to during different stages of pregnancy.
caveolin Binding (association) of maxi-K channel
2) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0.07 Pain Relevance 0
However, mutation of all three aromatic amino acids (mutant Y1007A, F1012A, Y1015A) was necessary to disrupt the association between caveolin and the maxi-K channel, as visualized by immunofluorescence and immunoprecipitation.


caveolin Binding (association) of maxi-K channel
3) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
To establish whether interactions between maxi-K channels and caveolin affect the endogenous myometrial total outward K+ current, we used a siRNA to inhibit cav-1 gene expression in hMSMCs.
caveolin Binding (interactions) of maxi-K
4) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
In spite of our knowledge of the existence of an association between the maxi-K channel and caveolin, how this interaction affects MSMC function remains unknown.
caveolin Binding (association) of maxi-K channel
5) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
Based on these findings, we believe that maxi-K channels that are present in caveolae and interact with caveolin would likewise be responsive to the negative effects of estrogen, and that the decrease in channel current expression could account for the more depolarized myometrial membrane and enhanced contractility during labor.
caveolin Binding (interact) of maxi-K
6) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
The interaction between the maxi-K channel and caveolin depends on a region in the channel's C-terminal caveolin-binding site.
caveolin Binding (interaction) of maxi-K channel
7) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
Maxi-K channels can reside in the caveolae, where they associate with the scaffolding protein caveolin [7,8].
caveolin Binding (associate) of Maxi-K
8) Confidence 0.01 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0

General Comments

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