INT100692

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Context Info
Confidence 0.78
First Reported 2002
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 6
Disease Relevance 3.42
Pain Relevance 1.70

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

cytosol (STAT6) signal transduction (STAT6) nucleolus (STAT6)
nucleus (STAT6) cytoplasm (STAT6) signal transducer activity (STAT6)
Anatomy Link Frequency
macrophages 1
dendritic cells 1
STAT6 (Homo sapiens)
Pain Link Frequency Relevance Heat
opioid receptor 9 98.44 Very High Very High Very High
Inflammation 208 96.52 Very High Very High Very High
Cannabinoid 8 95.96 Very High Very High Very High
chemokine 49 86.80 High High
cytokine 193 86.48 High High
mu opioid receptor 1 85.56 High High
aspirin 14 84.96 Quite High
antagonist 76 83.08 Quite High
Paracetamol 2 75.88 Quite High
agonist 47 75.00 Quite High
Disease Link Frequency Relevance Heat
Cancer 43 99.20 Very High Very High Very High
INFLAMMATION 223 96.52 Very High Very High Very High
General Immunology 4 94.80 High High
Breast Cancer 4 92.76 High High
Hypersensitivity 31 92.00 High High
Occupational Lung Diseases 30 91.76 High High
Disease 66 91.28 High High
Organ Transplantation 2 82.56 Quite High
Immunotherapy Of Cancer 2 80.40 Quite High
Communicable Diseases 5 74.40 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, we found that an Src kinase was involved in STAT6 activation because 1) Src kinase activity was induced by IL-4, 2) Src kinase activity, but not Janus kinase, was inhibited by salicylates in vitro, 3) cells expressing viral Src had constitutive STAT6 phosphorylation, and 4) cells lacking Src showed low STAT6 phosphorylation in response to IL-4.
Phosphorylation (phosphorylation) of STAT6
1) Confidence 0.78 Published 2002 Journal J. Immunol. Section Abstract Doc Link 11801685 Disease Relevance 0.53 Pain Relevance 0.25
Furthermore, we found that an Src kinase was involved in STAT6 activation because 1) Src kinase activity was induced by IL-4, 2) Src kinase activity, but not Janus kinase, was inhibited by salicylates in vitro, 3) cells expressing viral Src had constitutive STAT6 phosphorylation, and 4) cells lacking Src showed low STAT6 phosphorylation in response to IL-4.
Phosphorylation (phosphorylation) of STAT6
2) Confidence 0.78 Published 2002 Journal J. Immunol. Section Abstract Doc Link 11801685 Disease Relevance 0.48 Pain Relevance 0.24
Further experiments demonstrate that interleukin-4 then induces phosphorylation of STAT6, which directly transactivates the mu-opioid receptor gene.
Phosphorylation (phosphorylation) of STAT6 associated with opioid receptor
3) Confidence 0.71 Published 2006 Journal Mol. Pharmacol. Section Abstract Doc Link 16434616 Disease Relevance 0 Pain Relevance 0.89
Glucocorticoids, in vitro (a) inhibit IL-12 secretion from monocyte-macrophages and dendritic cells, (b) decrease IL-12 receptor 1- and 2-chain expression, thereby inhibiting IL-12 signaling, and (c) inhibit IL-12-induced STAT-4 (transcription factor that drives Th1 differentiation) phosphorylation without affecting STAT-6 (transcription factor that drives Th2 differentiation) phosphorylation (d), and thereby deviate the immune response predominantly toward the Th2 phenotype [8,12].
Phosphorylation (phosphorylation) of STAT-6 in dendritic cells
4) Confidence 0.29 Published 2008 Journal J Occup Med Toxicol Section Body Doc Link PMC2259400 Disease Relevance 0.43 Pain Relevance 0.11
The secreted IL-13 signals cancer cells as demonstrated by the presence of phosphorylated STAT-6 and contributes to tumor growth as demonstrated in humanized mice model described hereunder [8] (K Palucka, Baylor Institute for Immunology Research, TX).
Phosphorylation (phosphorylated) of STAT-6 associated with cancer and general immunology
5) Confidence 0.14 Published 2007 Journal J Transl Med Section Body Doc Link PMC2176053 Disease Relevance 1.55 Pain Relevance 0.09
Glucocorticoids, in vitro (a) inhibit IL-12 secretion from monocyte-macrophages and dendritic cells, (b) decrease IL-12 receptor 1- and 2-chain expression, thereby inhibiting IL-12 signaling, and (c) inhibit IL-12-induced STAT-4 (transcription factor that drives Th1 differentiation) phosphorylation without affecting STAT-6 (transcription factor that drives Th2 differentiation) phosphorylation (d), and thereby deviate the immune response predominantly toward the Th2 phenotype [8,12].
Phosphorylation (phosphorylation) of STAT-6 in macrophages
6) Confidence 0.10 Published 2008 Journal J Occup Med Toxicol Section Body Doc Link PMC2259400 Disease Relevance 0.43 Pain Relevance 0.11

General Comments

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