INT196782

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Context Info
Confidence 0.61
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 32
Total Number 32
Disease Relevance 1.89
Pain Relevance 4.33

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

cytosol (Ppp2ca) chromosome (Ppp2ca) plasma membrane (Ppp2ca)
cytoskeleton (Ppp2ca) nucleus (Ppp2ca) cytoplasm (Ppp2ca)
Anatomy Link Frequency
PP2A 2
M cell 1
olfactory bulbs 1
ventral 1
Ppp2ca (Mus musculus)
Pain Link Frequency Relevance Heat
midbrain 57 99.52 Very High Very High Very High
Dopamine 2679 98.24 Very High Very High Very High
Catecholamine 54 93.96 High High
Calcium channel 42 83.60 Quite High
Glutamate 651 76.72 Quite High
agonist 22 70.88 Quite High
Action potential 84 65.36 Quite High
nMDA receptor 42 55.68 Quite High
ischemia 25 52.56 Quite High
Substantia nigra 102 28.28 Quite Low
Disease Link Frequency Relevance Heat
Targeted Disruption 92 99.72 Very High Very High Very High
Apoptosis 166 99.52 Very High Very High Very High
Parkinson's Disease 169 93.92 High High
Reperfusion Injury 21 90.32 High High
Death 7 76.92 Quite High
Aging 45 64.64 Quite High
Cv Unclassified Under Development 24 52.56 Quite High
Cancer 8 48.92 Quite Low
Stress 22 48.28 Quite Low
Hypertension 2 40.16 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
It is known that prolonged activation of PP2A can induce apoptosis in part by enhancing pro-apoptotic Bax activity (105), which stimulates ceramide production, a factor also known to contribute to PD pathology (106).
Positive_regulation (activation) of PP2A associated with parkinson's disease and apoptosis
1) Confidence 0.61 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.36 Pain Relevance 0
ERK phosphorylation was diminished in a-Syn cells compared with GFP-transfected MN9D controls, and furthermore, inhibition of PP2A increased ERK phosphorylation in our cells (data not shown), suggesting that only a-Syn interacting proteins were affected by a-Syn-mediated PP2A activation.
Positive_regulation (activation) of PP2A
2) Confidence 0.44 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.05 Pain Relevance 0.04
These findings are supported by our in vivo studies (Figs. 3 and 6), suggesting the possibility that (i) TH inhibition may be caused by an up-regulation of PP2A activity that is triggered by a-Syn overexpression, (ii) PP2A activation and TH inhibition may be independently triggered by a-Syn overexpression leading to interactions that affect both enzymes, or (iii) that TH inhibition may be an additive consequence of a-Syn overexpression and its ability to activate PP2A.
Positive_regulation (activate) of PP2A
3) Confidence 0.44 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.11 Pain Relevance 0.06
The calcium pulse given simultaneously with the dopamine input also significantly enhances the decrease in phosphoThr75 (Figure 5E) due to the additional calcium-dependent activation of PP2A, which further elevates PP2A activity.
Positive_regulation (activation) of PP2A associated with dopamine
4) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.42
These differences between a brief, high-amplitude calcium input and a slower, low-amplitude calcium input are due to the different effects that these calcium signals have on the level of PP2B and PP2A activation.
Positive_regulation (activation) of PP2A
5) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.15
In contrast, the dephosphorylation of Thr75 is dependent on calcium activation of PP2A.
Positive_regulation (activation) of PP2A
6) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.18
If calcium is prevented from binding to and enhancing PP2A activity, then a transient calcium stimulation does not increase PKAc activity, but instead decreases PKAc.
Positive_regulation (enhancing) of PP2A
7) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0
If calcium activation of PP2A is eliminated, a calcium elevation does not affect the levels of phosphoThr75 much (Figure 2B2, dotted line).
Positive_regulation (activation) of PP2A
8) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.18
This prediction is tested with simulations in which the calcium-dependent enhancement of PP2A is eliminated (rate constants set to zero).
Positive_regulation (enhancement) of PP2A
9) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.22
Also, if the calcium activation is very slow, then very little calcium-dependent activation of PP2A occurs during the brief duration of the calcium inputs, and the effect of paired stimulation decreases.
Positive_regulation (activation) of PP2A
10) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.16
Steady-state calcium produces a large increase in PP2B, dephosphorylating phosphoThr34; in contrast, large, transient calcium elevations produce an increase in PP2A activation and consequent disinhibition of free PKAc due to phosphoThr75 dephosphorylation.
Positive_regulation (activation) of PP2A
11) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.03
But only the briefer and high concentration calcium activates PP2A significantly (Figure 7D, solid line).
Positive_regulation (activates) of PP2A
12) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.09
This implies that if calcium-dependent activation of PP2A is eliminated, but the PKA–PP2A–phosphoThr75 loop is kept intact, pairing calcium and dopamine will give smaller elevations of free PKAc and phosphoThr34, than dopamine alone.
Positive_regulation (activation) of PP2A associated with dopamine
13) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.20
In particular, the dissociation rate for calcium binding to AC5, calcium–calmodulin binding to PDE1, and calcium-dependent activation of PP2A is not known.
Positive_regulation (activation) of PP2A
14) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.17
The calcium pulse given simultaneously with the dopamine input also significantly enhances the decrease in phosphoThr75 (Figure 5E) due to the additional calcium-dependent activation of PP2A, which further elevates PP2A activity.
Positive_regulation (activation) of PP2A associated with dopamine
15) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.43
The model is mildly sensitive to the rate of calcium-dependent enhancement of PP2A activity.
Positive_regulation (enhancement) of PP2A
16) Confidence 0.44 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.22
When we measured PP2A activity in MN9D cells, we found significantly elevated PP2A activity in both WT-Syn and S129A-Syn cells compared with GFP-transfected controls, with the largest activation of PP2A noted for S129A-Syn dephosphorylation mimic cells (Fig. 5C; p < 0.0001, one-way ANOVA).
Positive_regulation (elevated) of PP2A
17) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0
In cells, a-Syn overexpression activates PP2A.
Positive_regulation (activates) of PP2A in PP2A
18) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2878529 Disease Relevance 0.14 Pain Relevance 0.13
Conversely, activity of PP2A was significantly elevated in ventral midbrain of WT-Syn- and S129A-Syn transduced mice compared with GFP lentivirus controls (Fig. 6D; p < 0.001, one-way ANOVA), with S129A again producing a bigger effect, much like our data from MN9D cells (Fig. 5).
Positive_regulation (elevated) of PP2A in ventral associated with midbrain
19) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0.12
When we measured PP2A activity in MN9D cells, we found significantly elevated PP2A activity in both WT-Syn and S129A-Syn cells compared with GFP-transfected controls, with the largest activation of PP2A noted for S129A-Syn dephosphorylation mimic cells (Fig. 5C; p < 0.0001, one-way ANOVA).
Positive_regulation (activation) of PP2A
20) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0

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