INT66987

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Context Info
Confidence 0.61
First Reported 1996
Last Reported 2010
Negated 2
Speculated 4
Reported most in Body
Documents 23
Total Number 27
Disease Relevance 7.86
Pain Relevance 6.80

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

cytosol (Th) mitochondrion (Th) oxidoreductase activity (Th)
nucleus (Th) cytoplasm (Th)
Anatomy Link Frequency
neuronal 3
brain 3
dopamine neurons 2
nucleus accumbens 1
striatum 1
Th (Mus musculus)
Pain Link Frequency Relevance Heat
Dopamine 553 100.00 Very High Very High Very High
cocaine 23 100.00 Very High Very High Very High
Morphine 16 100.00 Very High Very High Very High
dopamine receptor 11 99.84 Very High Very High Very High
Ventral tegmentum 44 98.62 Very High Very High Very High
Nucleus accumbens 27 98.56 Very High Very High Very High
Catecholamine 77 94.60 High High
Locus ceruleus 10 91.52 High High
Substantia nigra 126 89.88 High High
Spinal cord 64 89.56 High High
Disease Link Frequency Relevance Heat
Targeted Disruption 143 99.84 Very High Very High Very High
Stress 38 99.12 Very High Very High Very High
Restless Legs Syndrome 126 97.72 Very High Very High Very High
Parkinson's Disease 343 97.64 Very High Very High Very High
Gliosis 3 97.36 Very High Very High Very High
Urological Neuroanatomy 49 89.56 High High
Disease 148 87.76 High High
Apoptosis 47 85.96 High High
INFLAMMATION 70 85.24 High High
Toxicity 40 84.64 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Regulation of tyrosine hydroxylase promoter activity by chronic morphine in TH9.0-LacZ transgenic mice.
Regulation (Regulation) of tyrosine hydroxylase associated with targeted disruption and morphine
1) Confidence 0.61 Published 1998 Journal J. Neurosci. Section Title Doc Link 9822754 Disease Relevance 0.16 Pain Relevance 0.60
We investigated the regulation of tyrosine hydroxylase (TH), the rate limiting enzyme of dopamine synthesis, and found that this enzyme is regulated at the levels of mRNA, protein, trafficking as well as in its regional, cellular and subcellular organization.
Spec (investigated) Regulation (regulation) of tyrosine hydroxylase associated with dopamine
2) Confidence 0.60 Published 1998 Journal C. R. Seances Soc. Biol. Fil. Section Abstract Doc Link 10101608 Disease Relevance 0.08 Pain Relevance 0.56
We investigated the regulation of tyrosine hydroxylase (TH), the rate limiting enzyme of dopamine synthesis, and found that this enzyme is regulated at the levels of mRNA, protein, trafficking as well as in its regional, cellular and subcellular organization.
Spec (investigated) Regulation (regulation) of TH associated with dopamine
3) Confidence 0.60 Published 1998 Journal C. R. Seances Soc. Biol. Fil. Section Abstract Doc Link 10101608 Disease Relevance 0.08 Pain Relevance 0.56
Prenatal stress or corticosterone treatment have a lasting effect on typosine hydroxylase (TH) activity and adrenoligands binding in the mice brain.
Regulation (effect) of TH in brain associated with stress
4) Confidence 0.57 Published 1996 Journal Fiziol Zh Im I M Sechenova Section Abstract Doc Link 8963333 Disease Relevance 0.27 Pain Relevance 0.09
After 2 months, TH, DA, DOPAC, and reactive glia in the SNc were still altered in MPTPp-treated mice as compared to controls.
Regulation (altered) of TH associated with dopamine
5) Confidence 0.45 Published 2009 Journal Neurotox Res Section Abstract Doc Link 19526289 Disease Relevance 0.41 Pain Relevance 0.30
Taken together, the mouse data provide compelling support for a physiological contribution of a-Syn to the regulation of TH and PP2A in vivo.
Regulation (regulation) of TH
6) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.06 Pain Relevance 0.03
Therefore, this study was undertaken to 1) further elucidate the molecular mechanisms underlying the effects of a-Syn on TH, especially Ser-19 phosphorylation, which represents a key step in 14-3-3-mediated-TH activation, 2) determine the in vivo significance of a-Syn in TH regulation in transgenic overexpressing and null mice, and 3) assess if a-Syn Ser-129 phosphorylation affects a-Syn function toward PP2A or TH.
Regulation (regulation) of TH associated with targeted disruption
7) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.57 Pain Relevance 0
Therefore, the third aim of this study was to assess if phosphorylation of a-Syn, in particular of Ser-129, affected PP2A or TH activity in vitro or in vivo.
Regulation (affected) of TH
8) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.09 Pain Relevance 0
These data identify a close relationship between a-Syn levels and TH phosphorylation in vivo, which prompted us to measure for changes in TH activity.


Regulation (changes) of TH
9) Confidence 0.35 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.05 Pain Relevance 0
To determine whether reduced TH phosphorylation reflected changes in TH enzymatic activity in striatum, we evaluated 15 mice per condition using a well characterized TH activity assay with minor modifications.
Spec (whether) Regulation (changes) of TH in striatum
10) Confidence 0.35 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0
The above findings demonstrate an age-dependent inhibitory effect of dynorphins on striatal dopamine synthesis via modulation of TH activity.
Regulation (modulation) of TH associated with dopamine
11) Confidence 0.27 Published 2009 Journal Exp. Neurol. Section Abstract Doc Link 19500577 Disease Relevance 0.62 Pain Relevance 0.34
To study the possibility that upregulation of TH occurs at the transcriptional level, we investigated the effect of chronic morphine or cocaine treatment on the activity of the TH gene promoter (9.0 kb), coupled to the LacZ reporter gene, in transgenic mice.
Spec (investigated) Regulation (effect) of TH associated with targeted disruption, cocaine and morphine
12) Confidence 0.27 Published 1998 Journal J. Neurosci. Section Abstract Doc Link 9822754 Disease Relevance 0.17 Pain Relevance 0.75
Tyrosine hydroxylase (TH) is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to dihydroxyphenylalanine (DOPA), and is a rate-limiting enzyme.14 TH is found in the cytoplasm of noradrenergic and dopaminergic neuronal cells in the locus coeruleus, ventral tegmental area, substantia nigra, adrenal medulla, and sympathetic ganglia.15 The TH gene is located in 11p15.5.15,16 Activation of TH reflects the increase of dopamine production.
Regulation (responsible) of TH in neuronal associated with medulla, ventral tegmentum, dopamine, substantia nigra and locus ceruleus
13) Confidence 0.26 Published 2009 Journal Psychiatry Investigation Section Body Doc Link PMC2796069 Disease Relevance 0.90 Pain Relevance 0.40
To control for such potential differences in TH, we normalized TH-Ser(P)-19 to total TH in all experiments.
Regulation (control) of TH
14) Confidence 0.26 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0 Pain Relevance 0
Interestingly, PTEN ablation did not generate changes in TH optical density in the striatum or nucleus accumbens, suggesting an equal distribution of dopaminergic terminals between Pten KO and control animals.
Neg (not) Regulation (changes) of TH in nucleus accumbens associated with nucleus accumbens
15) Confidence 0.26 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2736587 Disease Relevance 0.24 Pain Relevance 0.51
We did not observe any alterations in the OB, striatal TH or brain tau protein levels as reported in other rotenone models [48], [50], [51], suggesting greater selectivity of the neuronal damage in our model.
Neg (not) Regulation (alterations) of TH in brain
16) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2808242 Disease Relevance 0.55 Pain Relevance 0.22
Tyrosine hydroxylase (TH) is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to dihydroxyphenylalanine (DOPA), and is a rate-limiting enzyme.14 TH is found in the cytoplasm of noradrenergic and dopaminergic neuronal cells in the locus coeruleus, ventral tegmental area, substantia nigra, adrenal medulla, and sympathetic ganglia.15 The TH gene is located in 11p15.5.15,16 Activation of TH reflects the increase of dopamine production.
Regulation (responsible) of Tyrosine hydroxylase in neuronal associated with medulla, ventral tegmentum, dopamine, substantia nigra and locus ceruleus
17) Confidence 0.22 Published 2009 Journal Psychiatry Investigation Section Body Doc Link PMC2796069 Disease Relevance 0.91 Pain Relevance 0.40
Tyrosine hydroxylase levels were unaltered, suggesting a dysregulation of dopamine activity rather than cell number.
Regulation (unaltered) of Tyrosine hydroxylase associated with dopamine
18) Confidence 0.20 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2276864 Disease Relevance 0 Pain Relevance 0.52
In vivo evidence, showing that a-Syn reduced Ser(P)-19 on TH, was obtained in transgenic mice expressing human a-Syn under the control of the TH-promoter (Syn++).
Regulation (control) of TH-promoter associated with targeted disruption
19) Confidence 0.18 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.30 Pain Relevance 0.11
Our studies using cell-free assays, dopaminergic neuronal cells, and four independent a-Syn mouse models have generated three major and novel findings regarding a-Syn-mediated regulation of TH and PP2A.
Regulation (regulation) of TH in neuronal
20) Confidence 0.18 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2878529 Disease Relevance 0.06 Pain Relevance 0.03

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