INT309735

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Context Info
Confidence 0.14
First Reported 2010
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 1
Total Number 14
Disease Relevance 0
Pain Relevance 0.75

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

plasma membrane (CALM3, TRPV4) nucleoplasm (CALM3) small molecule metabolic process (CALM3)
carbohydrate metabolic process (CALM3) transmembrane transport (TRPV4) cytoplasm (CALM3)
Anatomy Link Frequency
lobe 4
CALM3 (Homo sapiens)
TRPV4 (Homo sapiens)
Pain Link Frequency Relevance Heat
TRP channel 56 98.50 Very High Very High Very High
adenocard 14 89.48 High High
addiction 28 80.08 Quite High
agonist 42 74.88 Quite High
qutenza 14 42.00 Quite Low
imagery 14 5.00 Very Low Very Low Very Low

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Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To investigate which of the alternative interactions of the P2 peptide is relevant in the absence and presence of CaM binding to the TRPV4 C terminus, we performed a series of competition experiments (Fig. 7D,E).
CaM Binding (binding) of TRPV4
1) Confidence 0.14 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
Thus, in contrast to some other TRP channels, where CaM binding is present at nanomolar Ca2+ concentrations [4], [29], CaM binding to TRPV4 depends on Ca2+ concentrations above those in resting cells.
CaM Binding (binding) of TRPV4 associated with trp channel
2) Confidence 0.14 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
Using different experimental strategies, we have demonstrated that an interaction between an N-terminal and a C-terminal site in TRPV4 is present at nanomolar Ca2+ concentrations (Fig. 8A), but becomes disrupted secondary to CaM binding to the TRPV4 C terminus at micromolar Ca2+ concentrations (Fig. 8B).
CaM Binding (binding) of TRPV4
3) Confidence 0.14 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
In contrast to these findings, TRPV4 neither binds to CaM in Ca2+-free buffers, nor to CaM1234, and potentiation of its activity directly depends on CaM interaction triggered by a rise in Ca2+.
CaM1234 Binding (binds) of TRPV4
4) Confidence 0.12 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
In contrast to these findings, TRPV4 neither binds to CaM in Ca2+-free buffers, nor to CaM1234, and potentiation of its activity directly depends on CaM interaction triggered by a rise in Ca2+.
CaM Binding (binds) of TRPV4
5) Confidence 0.12 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.09
CaM mutants with a dysfunctional C lobe (CaM34, CaM1234) had no effect (Fig. 1F), probably because these mutants do not interact with the TRPV4 C-terminal domain and do not functionally compete with endogenous CaM.
CaM Neg (not) Binding (interact) of TRPV4 in lobe
6) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.06
CaM mutants with a dysfunctional C lobe (CaM34, CaM1234) had no effect (Fig. 1F), probably because these mutants do not interact with the TRPV4 C-terminal domain and do not functionally compete with endogenous CaM.
CaM34 Neg (not) Binding (interact) of TRPV4 in lobe
7) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.05
How does CaM binding facilitate Ca2+ entry through TRPV4 at the molecular level?
CaM Binding (binding) of TRPV4
8) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.08
Because CaM interaction with a C-terminal binding site in TRPV4 has been shown to be an essential step in the Ca2+-dependent potentiation of TRPV4 [11], we attempted to obtain initial clues about the underlying molecular mechanism by studying the CaM binding geometry.
CaM Binding (interaction) of TRPV4
9) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.06
The C-terminal CaM binding site in TRPV4 binds to the CaM C lobe
CaM Binding (binds) of TRPV4 in lobe
10) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.06
First, we did a complementation experiment to test whether a CaM molecule that binds to the C2 fragment of TRPV4 through its C-lobe can form an additional interaction with another CaM binding domain thus forming a ternary complex.
CaM Binding (binds) of TRPV4 in lobe
11) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0
Very high Ca2+ concentrations above 100 ┬ÁM, however, inhibited binding of the fragments, a process that is probably secondary to unspecific Ca2+ binding and has been observed for other protein interactions including CaM binding to TRPV4 [11].
CaM Binding (binding) of TRPV4
12) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.04
The first comprises a ternary interaction in which Ca2+-loaded CaM binds to two different sites within the TRPV4 protein thus bringing two regulatory domains in proximity to each other.
CaM Binding (binds) of TRPV4 protein
13) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07
Using protein interaction experiments and functional assays, we show that the molecular correlate of Ca2+-dependent current potentiation is disruption of an interdomain interaction within TRPV4 resulting from CaM binding to a C-terminal site.
CaM Binding (binding) of TRPV4
14) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2867956 Disease Relevance 0 Pain Relevance 0.07

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