INT230265

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Context Info
Confidence 0.42
First Reported 2006
Last Reported 2008
Negated 0
Speculated 1
Reported most in Body
Documents 2
Total Number 8
Disease Relevance 0.74
Pain Relevance 0.44

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

cell differentiation (Cav3) Golgi apparatus (Cav3) plasma membrane organization (Cav3)
plasma membrane (Cav3) enzyme binding (Cav3) protein complex (Cav3)
Anatomy Link Frequency
plasma 1
muscle cells 1
chondrocytes 1
Cav3 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
rheumatoid arthritis 14 81.36 Quite High
Osteoarthritis 28 79.36 Quite High
Inflammation 35 74.64 Quite High
COX-2 inhibitor 7 70.96 Quite High
Pain 7 67.52 Quite High
Arthritis 7 66.88 Quite High
repetitive firing 2 19.52 Low Low
Action potential 9 5.00 Very Low Very Low Very Low
hyperexcitability 4 5.00 Very Low Very Low Very Low
Hippocampus 3 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Rheumatoid Arthritis 14 81.36 Quite High
Osteoarthritis 28 79.36 Quite High
INFLAMMATION 21 74.64 Quite High
Pain 7 67.52 Quite High
Arthritis 21 66.88 Quite High
Epilepsy 17 6.96 Low Low
Stroke 7 5.00 Very Low Very Low Very Low
Volume Depletion And Dehydration 7 5.00 Very Low Very Low Very Low
Convulsion 3 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This result is consistent with their co-localization (Fig. 3), as well as the direct binding between COX-2 and Cav-3 in the caveolae-enriched membrane fractions.


Cav-3 Binding (binding) of
1) Confidence 0.42 Published 2006 Journal Journal of Korean Medical Science Section Body Doc Link PMC2733955 Disease Relevance 0 Pain Relevance 0
Normally, Cav-1 and Cav-2 are co-expressed and they form a hetero-oligomeric complex in many cell types (28, 29), but Cav-3 is known to be specific for muscle cells (30).
Cav-3 Binding (specific) of in muscle cells
2) Confidence 0.32 Published 2006 Journal Journal of Korean Medical Science Section Body Doc Link PMC2733955 Disease Relevance 0 Pain Relevance 0
The presence of the COX-2 and Cav-3 complexes could also be detected following precipitation with the Cav-3 antibody (Fig. 4B).
Cav-3 Binding (complexes) of
3) Confidence 0.32 Published 2006 Journal Journal of Korean Medical Science Section Body Doc Link PMC2733955 Disease Relevance 0 Pain Relevance 0
The reasons for this un-expected co-localization of COX-2 in the caveolae by its binding to Cav-3 are not clear.
Cav-3 Spec (clear) Binding (binding) of
4) Confidence 0.32 Published 2006 Journal Journal of Korean Medical Science Section Body Doc Link PMC2733955 Disease Relevance 0 Pain Relevance 0
The immuno-precipitation experiments showed complex formation between the COX-2 and Cav-3 in the rat chondrocytes.
Cav-3 Binding (formation) of in chondrocytes
5) Confidence 0.31 Published 2006 Journal Journal of Korean Medical Science Section Abstract Doc Link PMC2733955 Disease Relevance 0 Pain Relevance 0
With respect to Cav-3, there is a little information on the protein-protein interaction of Cav-3.
Cav-3 Binding (interaction) of
6) Confidence 0.31 Published 2006 Journal Journal of Korean Medical Science Section Body Doc Link PMC2733955 Disease Relevance 0.21 Pain Relevance 0.17
Several lines of evidences that were provided in the current study support this conclusion: 1) Western blot analysis of COX-2 indicated that it is present in the caveolae-enriched membrane fraction along with Cav-3, 2) the cross-over immuno-precipitation results show that the COX-2 protein formed a bound complex with the Cav-3 protein, and 3) with using confocal and electron microscopes, the immunocytochemistry images show that at least some portion of the COX-2 is co-localized with Cav-3 in the plasma membrane.
Cav-3 protein Binding (bound) of in plasma
7) Confidence 0.31 Published 2006 Journal Journal of Korean Medical Science Section Body Doc Link PMC2733955 Disease Relevance 0.53 Pain Relevance 0.26
Unlike the Migliore model of CA3 and the recent model of CA1 from Golomb et al., which rely on window or persistent Na+ current to enhance bistability of the fast subsystem as a bursting mechanism (see [23]), our model burst is generated as a result of the interaction of two slow variables, a slow autocatalytic variable n (CaV3.1 T-type Ca2+ channel activation gate) and a slow negative feedback variable o (Ca2+-dependent potassium (K+) channel activation gate); all other variables in our system are fast (and are insufficient to generate somatic bursts–see Figure 1C, middle panel).
CaV3 Binding (interaction) of
8) Confidence 0.02 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2323611 Disease Relevance 0 Pain Relevance 0

General Comments

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