INT90275

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.58
First Reported 2000
Last Reported 2011
Negated 0
Speculated 0
Reported most in Body
Documents 29
Total Number 29
Disease Relevance 1.91
Pain Relevance 7.11

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

mitochondrion (Ppp1cc) carbohydrate metabolic process (Ppp1cc) protein complex (Ppp1cc)
cytoplasm (Ppp1cc) chromosome (Ppp1cc) nucleolus (Ppp1cc)
Anatomy Link Frequency
brain 2
myometrium 1
Ppp1cc (Mus musculus)
Pain Link Frequency Relevance Heat
Kinase C 40 99.80 Very High Very High Very High
Dopamine 863 99.76 Very High Very High Very High
depression 104 99.56 Very High Very High Very High
abdominal pain 1 99.32 Very High Very High Very High
Glutamate 226 98.96 Very High Very High Very High
long-term potentiation 135 98.84 Very High Very High Very High
Nav1.6 70 98.36 Very High Very High Very High
Spinal cord 63 97.44 Very High Very High Very High
Neurotransmitter 33 97.04 Very High Very High Very High
Dismenorea 4 96.48 Very High Very High Very High
Disease Link Frequency Relevance Heat
Depression 104 99.56 Very High Very High Very High
Abdominal Pain 1 99.32 Very High Very High Very High
Stress 13 99.20 Very High Very High Very High
Vomiting 2 98.56 Very High Very High Very High
Diarrhoea 1 97.84 Very High Very High Very High
Dysmenorrhea 4 96.48 Very High Very High Very High
Bordatella Infection 3 89.12 High High
Targeted Disruption 143 85.52 High High
Neuroblastoma 4 80.00 Quite High
Disease 97 72.12 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
On the other hand, high doses of okadaic acid (10 ng/mouse, i.c.v.) and cantharidin (1 microg/mouse, i.c.v.), which also block PP1, and calyculin-A (0.1 fg/mouse-1 ng/mouse, i.c.v.), which inhibits equally both PP1 and PP2A, did not modify the morphine-induced antinociception.
Negative_regulation (block) of PP1 associated with antinociception and morphine
1) Confidence 0.58 Published 2003 Journal Eur. J. Pharmacol. Section Abstract Doc Link 12650833 Disease Relevance 0 Pain Relevance 1.09
These expression patterns point to possible roles for KEPI in regulating protein dephosphorylation by inhibiting PP1 activities in a number of brain pathways likely to use several different neurotransmitters and to participate in a number of brain functions.
Negative_regulation (inhibiting) of PP1 in brain associated with neurotransmitter
2) Confidence 0.57 Published 2005 Journal Neuroscience Section Abstract Doc Link 15837133 Disease Relevance 0 Pain Relevance 0.58
Mouse brain localization of the protein kinase C-enhanced phosphatase 1 inhibitor KEPI (kinase C-enhanced PP1 inhibitor).
Negative_regulation (inhibitor) of PP1 in brain associated with kinase c
3) Confidence 0.57 Published 2005 Journal Neuroscience Section Title Doc Link 15837133 Disease Relevance 0 Pain Relevance 0.44
In summary, these studies have indicated 1) that PP1 is the primary myometrial OA-sensitive PP; 2) that inhibition of PP1 had no effect on spontaneous contractions, whereas it markedly inhibited OT-stimulated uterine contractions; and 3) that PP1 is differentially expressed in the circular and longitudinal myometrium in relation to sexual development.
Negative_regulation (inhibition) of PP1 in myometrium associated with dismenorea
4) Confidence 0.55 Published 2000 Journal Biol. Reprod. Section Abstract Doc Link 10952921 Disease Relevance 0.16 Pain Relevance 0.16
For example, the inhibition of PP1 abolished LTD and activated LTP [15], [16], [37], [38].
Negative_regulation (inhibition) of PP1 associated with depression and long-term potentiation
5) Confidence 0.39 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2169299 Disease Relevance 0.41 Pain Relevance 0.30
OA is a potent inhibitor of protein phosphatase 1 (PP1) and 2A (PP2A), enzymes that are known to be critical regulators of embryonic development.
Negative_regulation (inhibitor) of PP1
6) Confidence 0.26 Published 2010 Journal Toxicon Section Abstract Doc Link 20026154 Disease Relevance 0.39 Pain Relevance 0.10
Thus, CaMKII autophosphorylation seems to augment the CaMKII activity soon after the [Ca2+]i increase, whereas the PDE1 inhibition pathway seems to attenuate the CaMKII inactivation later, presumably through suppressing the PP-1 activity.


Negative_regulation (suppressing) of PP-1
7) Confidence 0.19 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
When DARPP-32 is phosphorylated at Thr34 it binds to and inactivates PP1, with an affinity of 1 nM [14].
Negative_regulation (inactivates) of PP1
8) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.05
The increase in Thr34 phosphorylation in its turn decreases PP1 (Figure 5C), and thus the ratio of PKAc to PP1 is greatly enhanced (Figure 5D) compared with dopamine alone.
Negative_regulation (decreases) of PP1 associated with dopamine
9) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.36
In particular, D1 receptor activation, producing PKAc, phosphorylation of DARPP-32, and subsequent inhibition of PP1 activates kinases that phosphorylate AMPA channels [45], leading to synaptic potentiation.
Negative_regulation (inhibition) of PP1
10) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.33
Figure 8A and 8B shows that, over a large range of dissociation rates for calcium binding to AC5 or Ca4CaM binding to PDE1, the PKAc elevation and PP1 suppression in response to a dopamine signal is enhanced when dopamine is paired with calcium.
Negative_regulation (suppression) of PP1 associated with dopamine
11) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.21
Thus, model simulations suggest that PKA activation, phosphorylation of DARPP-32 at Thr34, and subsequent PP1 inhibition, produced by conjunctive glutamate and D1 receptor stimulation, can produce LTP by increased phosphorylation of AMPA receptors.
Negative_regulation (inhibition) of PP1 associated with glutamate and long-term potentiation
12) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.73
More significantly, combined dopamine and glutamate stimulation produces a larger activation of PKA and inhibition of PP1 than dopamine alone (Figure 5).
Negative_regulation (inhibition) of PP1 associated with glutamate and dopamine
13) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.24
When phosphorylated at Thr34, DARPP-32 is a potent inhibitor of PP1 [14], whereas when phosphorylated at Thr75 DARPP-32 inhibits protein kinase A (PKA) [15].
Negative_regulation (inhibitor) of PP1
14) Confidence 0.17 Published 2006 Journal PLoS Computational Biology Section Body Doc Link PMC1562452 Disease Relevance 0 Pain Relevance 0.38
In control experiments using the PP2A-specific inhibitor fostriecin (10 nm), low dose okadaic acid (50 nm), or the protein phosphatase 1 (PP1)-specific inhibitor protein phosphatase inhibitor-2 (PPI2, 50 nm), we verified that fostriecin and low dose okadaic acid could both inhibit phosphatase activity in our assay, whereas the PP1 inhibitor did not (not shown).
Negative_regulation (inhibitor) of PP1
15) Confidence 0.16 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0
DSLET-mediated ERK activation was significantly inhibited by the Src kinase inhibitor, PP1 (10 ?
Negative_regulation (inhibitor) of PP1
16) Confidence 0.15 Published 2002 Journal BMC Pharmacol Section Body Doc Link PMC88976 Disease Relevance 0 Pain Relevance 0.16
Thus, the positive-feedback loop consisting of PDE1 inhibition by CaMKII shifted the molecular network from a dephosphorylation-dominant state to a phosphorylation-dominant state through suppressing PP-1 activity.
Negative_regulation (suppressing) of PP-1
17) Confidence 0.14 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0.04
In summary, sustained CaMKII activation and GABAAR phosphorylation were accompanied by long-term decreases in the amounts of active PP-1 and PDE1 (Figure 2E and J), and by sustained increases in the amounts of phospho-DARPP-32, cAMP, and active PKA (Figure 2A, B, and G–I).
Negative_regulation (decreases) of PP-1
18) Confidence 0.14 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0.03
As the amount of active CaMKII increased, active PP-1 decreased in a manner depending on PDE1 phosphorylation by CaMKII (Figure 5F).
Negative_regulation (decreased) of PP-1
19) Confidence 0.14 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0
As a result, PP-1 was inhibited by phospho-DARPP-32 (see Figures 2 and 5).
Negative_regulation (inhibited) of PP-1
20) Confidence 0.14 Published 2009 Journal Mol Syst Biol Section Body Doc Link PMC2710870 Disease Relevance 0 Pain Relevance 0.03

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox