INT109450

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Context Info
Confidence 0.64
First Reported 2003
Last Reported 2011
Negated 4
Speculated 0
Reported most in Body
Documents 62
Total Number 62
Disease Relevance 25.18
Pain Relevance 4.21

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

cell differentiation (AKT1) nucleoplasm (AKT1) transport (AKT1)
small molecule metabolic process (AKT1) enzyme binding (AKT1) carbohydrate metabolic process (AKT1)
Anatomy Link Frequency
AsPC-1 6
muscle 4
cleavage 2
leg 2
T24 2
AKT1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Nicotine 80 99.98 Very High Very High Very High
aspirin 41 99.98 Very High Very High Very High
cINOD 107 99.58 Very High Very High Very High
antagonist 68 97.58 Very High Very High Very High
diclofenac 8 90.56 High High
Inflammation 221 90.32 High High
COX-2 inhibitor 115 89.64 High High
cytokine 118 88.40 High High
withdrawal 8 88.40 High High
Inflammatory response 26 81.92 Quite High
Disease Link Frequency Relevance Heat
Apoptosis 1069 100.00 Very High Very High Very High
Cancer 919 99.64 Very High Very High Very High
Pancreatic Cancer 152 99.60 Very High Very High Very High
Colon Cancer 88 99.24 Very High Very High Very High
Endometrial Cancer 339 99.00 Very High Very High Very High
Hypoxia 82 98.84 Very High Very High Very High
Hemangiosarcoma 139 98.46 Very High Very High Very High
Neuroblastoma 9 97.88 Very High Very High Very High
Glioma 26 97.04 Very High Very High Very High
Disease 116 96.56 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The phosphorylation of a conserved threonine residue (Thr308 in Akt1, Thr309 in Akt2 and Thr305 in Akt3), upon growth factor stimulation, is required for Akt activation, while the phosphorylation of a serine residue (Ser473 in Akt1, Ser474 in Akt2 and Ser474 in Akt3) is only required for maximal Akt activity [21,24-26].
Positive_regulation (required) of Phosphorylation (phosphorylation) of Akt1
1) Confidence 0.64 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.43 Pain Relevance 0.04
Cyclic AMP, an inducer of Akt phosphorylation, suppresses Akt inactivation, Bid cleavage, and DNA fragmentation.
Positive_regulation (inducer) of Phosphorylation (phosphorylation) of Akt in cleavage
2) Confidence 0.64 Published 2004 Journal Free Radic. Biol. Med. Section Abstract Doc Link 15451068 Disease Relevance 0.54 Pain Relevance 0.39
In fact, we have shown that NSAIDs, in some instances, increase Akt phosphorylation in human pancreatic carcinoma cells suggesting activation of the phosphatidylinositol 3'-kinase (PI3K)-Akt survival (antiapoptotic) pathway.
Positive_regulation (increase) of Phosphorylation (phosphorylation) of Akt associated with pancreatic cancer and cinod
3) Confidence 0.61 Published 2003 Journal J. Gastrointest. Surg. Section Abstract Doc Link 12654560 Disease Relevance 0.54 Pain Relevance 0.44
Immunohistochemical staining using an anti-phosphorylated-AKT antibody showed that phosphorylated (activated) AKT was expressed in cancer cells but not in neighboring normal mucosa in 16 cases (84.2%).
Positive_regulation (activated) of Phosphorylation (phosphorylated) of AKT associated with cancer
4) Confidence 0.50 Published 2004 Journal Cancer Res. Section Abstract Doc Link 15150102 Disease Relevance 1.00 Pain Relevance 0.14
Our results (Figure 5-B) indicate that Src is required for both serine and threonine phosphorylation of Akt, the PI3 kinase pathway is required for threonine phosphorylation of Akt and mTOR Complex 2 is required for serine phosphorylation of Akt.
Positive_regulation (required) of Phosphorylation (phosphorylation) of Akt
5) Confidence 0.45 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2831839 Disease Relevance 0 Pain Relevance 0
Our results (Figure 5-B) indicate that Src is required for both serine and threonine phosphorylation of Akt, the PI3 kinase pathway is required for threonine phosphorylation of Akt and mTOR Complex 2 is required for serine phosphorylation of Akt.
Positive_regulation (required) of Phosphorylation (phosphorylation) of Akt
6) Confidence 0.45 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2831839 Disease Relevance 0 Pain Relevance 0
In vitro studies showed that activating mutations of PIK3CA in combination with PTEN mutations led to an additional increase in phosphorylated AKT when compared with cells with only inactivated PTEN [6].
Positive_regulation (increase) of Phosphorylation (phosphorylated) of AKT
7) Confidence 0.43 Published 2010 Journal Obstetrics and Gynecology International Section Body Doc Link PMC2846683 Disease Relevance 0.43 Pain Relevance 0
As we showed previously, mutated PTEN endometrial cancer cell lines (RL 95-2 and Ishikawa) expressed high levels of Akt phosphorylation which was concomitant with the presence of high levels of COX-2 mRNA and protein [42].
Positive_regulation (levels) of Phosphorylation (phosphorylation) of Akt associated with endometrial cancer
8) Confidence 0.43 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.60 Pain Relevance 0
On the opposite, the presence of a mutated PTEN protein enables Akt phosphorylation, which in turn may phosphorylate I?
Positive_regulation (enables) of Phosphorylation (phosphorylation) of Akt
9) Confidence 0.43 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.23 Pain Relevance 0
In the presence of a mutated PTEN protein, Akt phosphorylation levels increase leading to the activation of this survival pathway.
Positive_regulation (increase) of Phosphorylation (phosphorylation) of Akt
10) Confidence 0.43 Published 2004 Journal Mol Cancer Section Abstract Doc Link PMC394342 Disease Relevance 0.78 Pain Relevance 0.13
may be other different targets following Akt phosphorylation to activate cell survival through COX-2 gene expression and PGE2 secretion.
Positive_regulation (activate) of Phosphorylation (phosphorylation) of Akt
11) Confidence 0.43 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.50 Pain Relevance 0.04
We have demonstrated previously that Akt is constitutively phosphorylated/activated in two mutated-PTEN human endometrial cancer cell lines that have been used in the present study (RL 95-2 and Ishikawa) [32,42].
Positive_regulation (activated) of Phosphorylation (phosphorylated) of Akt associated with endometrial cancer
12) Confidence 0.43 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.29 Pain Relevance 0.04
may be other different targets following Akt phosphorylation to activate cell survival through COX-2 gene expression and PGE2 secretion.
Positive_regulation (following) of Phosphorylation (phosphorylation) of Akt
13) Confidence 0.43 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.50 Pain Relevance 0.04
PTEN is a crucial phosphatase involved in the regulation of Akt phosphorylation: the presence of an active PTEN protein blocks Akt phosphorylation by the dephosphorylation of PI 3-K product, PIP3 [45].
Positive_regulation (active) of Phosphorylation (phosphorylation) of Akt
14) Confidence 0.43 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.29 Pain Relevance 0.04
Dominant negative Akt vector blocked IkB phosphorylation, which leads to the activation of apoptosis
Positive_regulation (negative) of Phosphorylation (phosphorylation) of Akt vector associated with apoptosis
15) Confidence 0.37 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.24 Pain Relevance 0
Dominant negative Akt vector blocked IkB phosphorylation, which leads to the activation of apoptosis
Positive_regulation (leads) of Phosphorylation (phosphorylation) of Akt vector associated with apoptosis
16) Confidence 0.37 Published 2004 Journal Mol Cancer Section Body Doc Link PMC394342 Disease Relevance 0.24 Pain Relevance 0
Data of Western blot further demonstrated that aspirin treatment caused activation of caspases, down-regulation of Mcl-1 protein, dephosphorylation of ERK-1/2 and AKT, and also IkappaB-alpha proteolysis-dependent NF-kappaB activation in YD-8 cells.
Positive_regulation (activation) of Phosphorylation (dephosphorylation) of AKT associated with aspirin
17) Confidence 0.35 Published 2010 Journal Toxicol In Vitro Section Abstract Doc Link 20116423 Disease Relevance 0.64 Pain Relevance 0.65
8 M nicotine induced the phosphorylation of Akt, suggesting an effect of nAChR activation on these signaling molecules.
Positive_regulation (induced) of Phosphorylation (phosphorylation) of Akt associated with nicotine
18) Confidence 0.34 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2737633 Disease Relevance 0.99 Pain Relevance 0.42
Our results (Figure 5-B) indicate that Src is required for both serine and threonine phosphorylation of Akt, the PI3 kinase pathway is required for threonine phosphorylation of Akt and mTOR Complex 2 is required for serine phosphorylation of Akt.
Positive_regulation (required) of Phosphorylation (phosphorylation) of Akt
19) Confidence 0.33 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2831839 Disease Relevance 0 Pain Relevance 0
Akt can also be threonine phosphorylated by PI3 kinase activation of PDK1 [41-45].
Positive_regulation (activation) of Phosphorylation (phosphorylated) of Akt
20) Confidence 0.33 Published 2010 Journal J Angiogenes Res Section Body Doc Link PMC2831839 Disease Relevance 0 Pain Relevance 0.32

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