INT200322

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Context Info
Confidence 0.39
First Reported 2006
Last Reported 2006
Negated 0
Speculated 1
Reported most in Body
Documents 1
Total Number 20
Disease Relevance 2.93
Pain Relevance 3.98

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

nucleus (Rest, Sp3) intracellular (Rest, Sp3) DNA binding (Rest, Sp3)
cytosol (Rest) protein complex (Rest) transcription factor binding (Rest)
Anatomy Link Frequency
neuronal 3
NS20Y 3
internal 1
nucleus 1
Rest (Mus musculus)
Sp3 (Mus musculus)
Pain Link Frequency Relevance Heat
mu opioid receptor 1600 99.84 Very High Very High Very High
Central nervous system 20 41.20 Quite Low
opioid receptor 60 8.32 Low Low
Morphine 60 5.00 Very Low Very Low Very Low
Glutamate receptor 20 5.00 Very Low Very Low Very Low
Analgesic 20 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Repression 280 100.00 Very High Very High Very High
Disease 80 100.00 Very High Very High Very High
Targeted Disruption 40 79.72 Quite High
Neurodegenerative Disease 20 65.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Our results have showed that Sp3 specifically binds to this mouse GC box and interacts with NRSF to synergistically repress the MOR expression.


NRSF Binding (interacts) of Sp3 associated with mu opioid receptor
1) Confidence 0.39 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.40 Pain Relevance 0.10
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.
NRSF Binding (interacts) of Sp3 factor associated with mu opioid receptor
2) Confidence 0.39 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0 Pain Relevance 0.16
Sp3 interacts with NRSF and binds G/C box adjacent to NRSE to repress transcription of MOR gene
NRSF Binding (interacts) of Sp3 associated with mu opioid receptor
3) Confidence 0.39 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.06 Pain Relevance 0.17
However, our current and previous data strongly suggest that the regulatory action of Sp3 factors is promoter- and cellular context dependent at least in the MOR gene expression because (i) only the full-length Sp3 can interact with NRSF in co-immunoprecipitation experiment whereas all three isoforms of Sp3 are expressed in NS20Y cells (Figure 4C), (ii) two short isoforms of Sp3 act as repressors by binding to the promoter element located at ?
NRSF Binding (interact) of Sp3 in NS20Y associated with mu opioid receptor
4) Confidence 0.39 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.16 Pain Relevance 0.19
In addition, immunoprecipitation experiment revealed that only the full-length Sp3 factor, other than two short Sp3 isoforms (M1 and M2), interact with NRSF (Figure 4C).
NRSF Binding (interact) of Sp3 factor
5) Confidence 0.34 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.18
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.
NRSF Binding (interacts) of Sp3 in nucleus
6) Confidence 0.34 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.13 Pain Relevance 0.09
Because two short isoforms are generated by internal start codon, it can be speculated that the N-terminal region (112 amino acid residues) of Sp3, which is absent from the two short isoforms, takes responsibility for the interaction of the full-length Sp3 with NRSF and for determining the role of Sp3 factors for MOR gene expression.
NRSF Binding (interaction) of Sp3 in internal associated with mu opioid receptor
7) Confidence 0.30 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.06 Pain Relevance 0.17
It is probable that the silencing of NRSF target genes in Huntinton's disease could also be the result of additive or synergic repression through increasing interaction with Sp3 or other transcriptional factors resulting from abnormal presence of NRSF in neuronal cells.
NRSF Binding (interaction) of Sp3 in neuronal associated with repression and disease
8) Confidence 0.30 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.82 Pain Relevance 0.07
In conjunction with our current data, especially from the co-immunoprecipitation of Sp3 with NRSF, it can be postulated that the involvement of Sp3 is needed for the full repression of MOR gene in addition to NRSF.
NRSF Binding (immunoprecipitation) of Sp3 associated with repression and mu opioid receptor
9) Confidence 0.30 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.17 Pain Relevance 0.15
In addition, immunoprecipitation experiment revealed that only the full-length Sp3 factor, other than two short Sp3 isoforms (M1 and M2), interact with NRSF (Figure 4C).
NRSF Binding (interact) of Sp3
10) Confidence 0.30 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.09 Pain Relevance 0.17
Evidence of the neuron-restrictive silencer factor (NRSF) interaction with Sp3 and its synergic repression to the mu opioid receptor (MOR) gene

Previously, we reported that the neuron-restrictive silencer element (NRSE) of mu opioid receptor (MOR) functions as a critical regulator to repress the MOR transcription in specific neuronal cells, depending on neuron-restriction silence factor (NRSF) expression levels [C.S.Kim, C.K.Hwang, H.S.Choi, K.Y.Song, P.Y.Law, L.N.Wei and H.H.Loh (2004) J.

NRSF Binding (interaction) of Sp3 in neuronal associated with repression and mu opioid receptor
11) Confidence 0.29 Published 2006 Journal Nucleic Acids Research Section Title Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.34
Evidence of the neuron-restrictive silencer factor (NRSF) interaction with Sp3 and its synergic repression to the mu opioid receptor (MOR) gene

Previously, we reported that the neuron-restrictive silencer element (NRSE) of mu opioid receptor (MOR) functions as a critical regulator to repress the MOR transcription in specific neuronal cells, depending on neuron-restriction silence factor (NRSF) expression levels [C.S.Kim, C.K.Hwang, H.S.Choi, K.Y.Song, P.Y.Law, L.N.Wei and H.H.Loh (2004) J.

neuron-restrictive silencer factor Binding (interaction) of Sp3 in neuronal associated with repression and mu opioid receptor
12) Confidence 0.29 Published 2006 Journal Nucleic Acids Research Section Title Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.34
The endogenous Sp3 factor and NRSF were co-immunoprecipitated with NRSF and Sp3 antibody, respectively.
NRSF Binding (immunoprecipitated) of Sp3 factor
13) Confidence 0.29 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.08 Pain Relevance 0.16
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).
NRSF Binding (interaction) of Sp3 in NS20Y associated with repression and mu opioid receptor
14) Confidence 0.29 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.15
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).
NRSF Binding (binds) of Sp3 in NS20Y associated with repression and mu opioid receptor
15) Confidence 0.29 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.10 Pain Relevance 0.16
The results suggest that the synergic interaction between NRSF and Sp3 is required to negatively regulate MOR gene transcription and that transcription of MOR gene would be governed by the context of available transcription factors rather than by a master regulator.



NRSF Binding (interaction) of Sp3 associated with mu opioid receptor
16) Confidence 0.29 Published 2006 Journal Nucleic Acids Research Section Abstract Doc Link PMC1702488 Disease Relevance 0.07 Pain Relevance 0.38
Although the exact mechanism of interdependency (or cooperativity) between NRSF and Sp3 for binding to NRSE/GC box remains to be elucidated, it is tempting to speculate that the function of Sp3 could be determined by the interaction with NRSF.
NRSF Spec (determined) Binding (interaction) of Sp3
17) Confidence 0.26 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.12 Pain Relevance 0.10
To our knowledge, this is the first report showing that the sequence-specific transcription factor (NRSF) has a differential interaction among Sp3 isoforms to regulate gene expression.
NRSF Binding (interaction) of Sp3
18) Confidence 0.26 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1702488 Disease Relevance 0.12 Pain Relevance 0.20
In the co-immunoprecipitation experiment, NRSF interacted with the full-length Sp3 factor, but not with Sp1 or two short Sp3 isoforms.
NRSF Binding (interacted) of Sp3
19) Confidence 0.25 Published 2006 Journal Nucleic Acids Research Section Abstract Doc Link PMC1702488 Disease Relevance 0.07 Pain Relevance 0.35
In the co-immunoprecipitation experiment, NRSF interacted with the full-length Sp3 factor, but not with Sp1 or two short Sp3 isoforms.
NRSF Binding (interacted) of Sp3 factor
20) Confidence 0.25 Published 2006 Journal Nucleic Acids Research Section Abstract Doc Link PMC1702488 Disease Relevance 0.07 Pain Relevance 0.35

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