INT198736

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Context Info
Confidence 0.40
First Reported 2006
Last Reported 2008
Negated 0
Speculated 3
Reported most in Body
Documents 23
Total Number 40
Disease Relevance 4.77
Pain Relevance 4.42

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nucleus (Sp3) intracellular (Sp3) DNA binding (Sp3)
Anatomy Link Frequency
NS20Y 5
macrophages 2
proximal 2
neuronal 1
nucleus 1
Sp3 (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 224 99.70 Very High Very High Very High
mu opioid receptor 1654 98.64 Very High Very High Very High
Glutamate receptor 20 90.24 High High
Inflammation 95 84.84 Quite High
chemokine 2 80.16 Quite High
Inflammatory response 52 80.04 Quite High
agonist 2 48.60 Quite Low
IPN 17 47.60 Quite Low
Pain 17 46.88 Quite Low
Central nervous system 44 41.20 Quite Low
Disease Link Frequency Relevance Heat
Repression 280 99.60 Very High Very High Very High
Disease 132 98.40 Very High Very High Very High
Apoptosis 3 94.96 High High
Obesity 34 91.44 High High
Atherosclerosis 187 88.24 High High
Cancer 27 86.48 High High
Necrosis 20 86.00 High High
INFLAMMATION 147 84.84 Quite High
Targeted Disruption 158 79.72 Quite High
Diabetes Mellitus 17 78.36 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The results clearly demonstrated that Sp3 factor binds the G/C motif and interacts with NRSF in MOR promoter region, suggesting that transcription factor Sp3 is required for silencing MOR expression together with NRSF.
Sp3 factor Binding (binds) of associated with mu opioid receptor
1) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.16
Our results have showed that Sp3 specifically binds to this mouse GC box and interacts with NRSF to synergistically repress the MOR expression.


Sp3 Binding (binds) of associated with mu opioid receptor
2) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.40 Pain Relevance 0.10
The same result was obtained using c-Myc-tagged NRSF expressed in NS20Y cells implying that Sp3 binds the GC box and a direct interaction between Sp3 and NRSF is required for a synergistic repression of MOR gene expression (Figure 4B).
Sp3 Binding (binds) of in NS20Y associated with repression and mu opioid receptor
3) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.16
In other words, if NRSF is abundant in the nucleus, Sp3 interacts with NRSF mainly acting as a repressor while, when NRSF is depleted in the nucleus or inactive, Sp3 might bind to the positive elements and act as a part of Sp1/Sp3 activator complex.
Sp3 Spec (might) Binding (bind) of in nucleus
4) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.15 Pain Relevance 0.06
Sp3 interacts with NRSF and binds G/C box adjacent to NRSE to repress transcription of MOR gene
Sp3 Binding (binds) of associated with mu opioid receptor
5) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.06 Pain Relevance 0.17
The same result was obtained using c-Myc-tagged NRSF expressed in NS20Y cells implying that Sp3 binds the GC box and a direct interaction between Sp3 and NRSF is required for a synergistic repression of MOR gene expression (Figure 4B).
Sp3 Binding (binds) of in NS20Y associated with repression and mu opioid receptor
6) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.16
The self NRSP competitor competed for protein–DNA interaction efficiently (lane 3) and also mutated competitor NRmSP and NRSPm significantly competed for upper complex indicating the specific binding of NRSF and Sp3 (lanes 7 and 8).
Sp3 Binding (binding) of in upper
7) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.06
Then, the specific and functional binding of Sp3 factor to the GC box was confirmed by gel-shift assays using either in vitro translated NRSF and Sp3 factor (Figure 5) or nuclear extract (Figure 6), and in vivo ChIP assay (Figure 7).
Sp3 factor Binding (binding) of
8) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.15
Taken altogether, the co-immunoprecipitation and EMSA studies demonstrate that NRSF and Sp3 factor interact with each other and physically bind to the repressive element of the MOR promoter, NRSE/GC box.


Sp3 factor Binding (interact) of associated with mu opioid receptor
9) Confidence 0.40 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.17
is mediated through decreased binding of Sp1 and Sp3 [29].
Sp3 Binding (binding) of
10) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0.04
PKB-mediated phosphorylation of rhSp1 had no effect on DNA binding (data not shown), thereby suggesting that a downstream kinase(s) was potentially mediating the actions of PKB on Sp1/Sp3 binding.
Sp1/Sp3 Binding (binding) of
11) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0.03
-mediated decrease in Sp1/Sp3 binding was analysed by EMSA.
Sp1/Sp3 Spec (analysed) Binding (binding) of
12) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0.05
-mediated suppression of Sp1/Sp3 binding (Fig. 7C).
Sp1/Sp3 Binding (binding) of
13) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0.03
-mediated reduction in Sp1/Sp3 binding.
Sp1/Sp3 Binding (binding) of
14) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0.39 Pain Relevance 0.05
-mediated decrease in Sp1/Sp3 binding to regulatory sequences in the gene [9].
Sp1/Sp3 Binding (binding) of
15) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0.22 Pain Relevance 0.14
Phosphorylation of extracts from untreated cells with two different concentrations of CK2 reduced the binding of Sp1/Sp3 to levels observed in IFN-?
Sp1/Sp3 Binding (binding) of
16) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0
As shown in Fig. 7D, rapamycin attenuated the decrease in Sp1/Sp3 binding.


Sp1/Sp3 Binding (binding) of
17) Confidence 0.32 Published 2008 Journal Cell Signal Section Body Doc Link PMC2586094 Disease Relevance 0 Pain Relevance 0.04
After cross-linking the proteins and DNAs with formaldehyde, cell lysates from NS20Y cells were subjected to immunoprecipitation with NRSF, HDAC1, HDAC2, Sp1, Sp3 and IRF-4 (as a negative control).
Sp3 Binding (immunoprecipitation) of in NS20Y
18) Confidence 0.31 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.25
The signal left after the treatment of the mutated competitor represents the complex with either NRSF (lane 7) or Sp3 (lane 8).
Sp3 Binding (represents) of
19) Confidence 0.31 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.03
300 residues from the translation start site while Sp3 has a minor effect by binding to one of these elements (25).
Sp3 Binding (binding) of
20) Confidence 0.31 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.35

General Comments

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