INT288582

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Context Info
Confidence 0.11
First Reported 2009
Last Reported 2009
Negated 1
Speculated 0
Reported most in Abstract
Documents 1
Total Number 15
Disease Relevance 0
Pain Relevance 0.22

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) Golgi apparatus (Cav1)
Anatomy Link Frequency
uterine 2
fibroblasts 1
Cav1 (Mus musculus)
Kcnma1 (Mus musculus)
Pain Link Frequency Relevance Heat
potassium channel 30 92.04 High High
anesthesia 15 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Stress 15 33.84 Quite Low
Infection 15 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Disruption of the maxi-K channel's association with caveolin-1 in mouse fibroblasts leads to channel mislocalization
caveolin-1 Binding (association) of maxi-K channel's in fibroblasts
1) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
Our results suggest that disruption of the caveolin-binding site interferes with the cav-1/maxi-K channel interaction, and that lack of the cav-1/maxi-K channel interaction in MSMCs attenuates the total K+ channel current of the cell.



cav-1 Binding (interaction) of maxi-K channel
2) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
The aim of this study was to investigate the consequences of this interaction - more specifically, how disruption of the association between the maxi-K channel and cav-1 may influence the current expression and excitability of myometrial cells - with the aim of better understanding the mechanisms that underlie the regulation of normal and aberrant uterine function.


cav-1 Binding (association) of maxi-K channel in uterine
3) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0.04
In this study we investigate the consequences of this interaction--more specifically, how the association between the maxi-K channel and cav-1 influences the current expression and excitability of myometrial cells--with the aim of better understanding the mechanisms that underlie the regulation of normal and aberrant uterine function.


cav-1 Binding (association) of maxi-K channel in uterine
4) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
To confirm that the reduction in maxi-K current observed in cells expressing the triple mutant is due to the altered interaction between the maxi-K channel and cav-1, we immunoprecipitated the maxi-K proteins from isolated lipid rafts (as indicated by a box in Figure 4).
cav-1 Binding (interaction) of maxi-K channel
5) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
These findings suggest that cav-1 contributes to the regulation of maxi-K current, at least in part, via specific maxi-K-caveolin interactions.


cav-1 Binding (interactions) of maxi-K-caveolin
6) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
These findings suggest that all three aromatic amino acids contribute to the interaction between the maxi-K channel and cav-1, but that two are sufficient to promote a detectable interaction.


cav-1 Binding (interaction) of maxi-K channel
7) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
A recent study investigating similar maxi-K channel mutants in HEK 293 cells found that single, double and triple substitutions of these aromatic amino acids fail to disrupt the interaction between the maxi-K channel and cav-1, but that complete deletion of the consensus site abolishes almost all (80-85%) interaction with cav-1 [8].
cav-1 Neg (fail) Binding (interaction) of maxi-K channel
8) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
In MSMCs, maxi-K channels can reside in the caveolae, where they associate with the scaffolding protein caveolin-1 (cav-1).
cav-1 Binding (associate) of maxi-K
9) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0.04
Our results suggest that disruption of the caveolin-binding site interferes with the cav-1/maxi-K channel interaction, and that lack of the cav-1/maxi-K channel interaction in MSMCs attenuates the total K+ channel current of the cell.



cav-1 Binding (interaction) of maxi-K channel
10) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
Our results suggest that disruption of the caveolin-binding site interferes with the cav-1/maxi-K channel interaction, and that lack of the cav-1/maxi-K channel interaction in MSMCs attenuates the total K+ channel current of the cell.



cav-1 Binding (interaction) of maxi-K channel
11) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
Our results suggest that disruption of the caveolin-binding site interferes with the cav-1/maxi-K channel interaction, and that lack of the cav-1/maxi-K channel interaction in MSMCs attenuates the total K+ channel current of the cell.



cav-1 Binding (interaction) of maxi-K channel
12) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
In MSMCs, maxi-K channels can reside in the caveolae, where they associate with the scaffolding protein caveolin-1 (cav-1).
caveolin-1 Binding (associate) of maxi-K
13) Confidence 0.11 Published 2009 Journal Reprod Biol Endocrinol Section Abstract Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0.04
Disruption of the maxi-K-caveolin-1 interaction alters current expression in human myometrial cells

Background

caveolin-1 Binding (interaction) of maxi-K
14) Confidence 0.09 Published 2009 Journal Reprod Biol Endocrinol Section Title Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0.05
Disruption of the maxi-K-caveolin-1 interaction alters current expression in human myometrial cells

Background

caveolin-1 Binding (interaction) of maxi-K
15) Confidence 0.09 Published 2009 Journal Reprod Biol Endocrinol Section Title Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0.05

General Comments

This test has worked.

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