INT97245

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Context Info
Confidence 0.77
First Reported 2001
Last Reported 2011
Negated 4
Speculated 4
Reported most in Body
Documents 217
Total Number 224
Disease Relevance 119.63
Pain Relevance 15.59

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
HeLa 8
HT-1080 4
RL95-2 3
keratinocyte 3
liver 3
AKT1 (Homo sapiens)
AKT1 - K179M (1)
Pain Link Frequency Relevance Heat
Nicotine 399 99.84 Very High Very High Very High
local anesthetic 11 99.60 Very High Very High Very High
aspirin 48 99.54 Very High Very High Very High
Osteoarthritis 321 99.24 Very High Very High Very High
Opioid 13 99.08 Very High Very High Very High
cva 44 99.04 Very High Very High Very High
Inflammation 416 98.92 Very High Very High Very High
Morphine 16 98.24 Very High Very High Very High
agonist 86 97.90 Very High Very High Very High
metalloproteinase 142 97.36 Very High Very High Very High
Disease Link Frequency Relevance Heat
Apoptosis 4357 100.00 Very High Very High Very High
Targeted Disruption 90 100.00 Very High Very High Very High
Cancer 4699 99.84 Very High Very High Very High
Hepatitis 199 99.84 Very High Very High Very High
Stress 232 99.76 Very High Very High Very High
Hypoxia 190 99.72 Very High Very High Very High
Glioblastoma 132 99.72 Very High Very High Very High
Cirrhosis 342 99.56 Very High Very High Very High
Cataract 342 99.54 Very High Very High Very High
Cervical Cancer 209 99.42 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
First, to examine whether activated AKT is expressed in BDCs, tumor specimens were obtained from 19 consecutive BDC cases.
Gene_expression (expressed) of AKT associated with bile duct neoplasms and cancer
1) Confidence 0.77 Published 2004 Journal Cancer Res. Section Abstract Doc Link 15150102 Disease Relevance 0.95 Pain Relevance 0.15
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%).
Neg (not) Gene_expression (expressed) of AKT associated with cancer
2) Confidence 0.77 Published 2004 Journal Cancer Res. Section Abstract Doc Link 15150102 Disease Relevance 1.00 Pain Relevance 0.13
A biological ISEL sub-study was performed including the assessment of EGFR gene copy number by fluorescent in situ hybridization (FISH), EGFR and p-AKT protein expression by immunohistochemistry (IHC), EGFR, K-RAS and B-RAF mutational status (Figure 1).31 It showed that a high EGFR gene copy number in patients treated with gefitinib represents a predictive factor of survival benefit when compared with placebo (HR: 0.61 versus 1.16 for high and low gene copy number, respectively; interaction test, P = 0.045), such as EGFR expression (HR: 0.77 versus 1.57 for positive and negative protein expression, respectively; interaction test, P = 0.049) (Table 1).
Gene_expression (expression) of AKT
3) Confidence 0.75 Published 2010 Journal Drug design, development and therapy Section Body Doc Link PMC2880339 Disease Relevance 0.06 Pain Relevance 0
However, expression of a constitutive active form of Akt/PKB (myristoylated PKB) has a low protective effect toward celecoxib-induced cell death.
Gene_expression (expression) of Akt associated with death
4) Confidence 0.75 Published 2002 Journal J. Biol. Chem. Section Abstract Doc Link 12000750 Disease Relevance 0.82 Pain Relevance 0.07
In the presence of IND 12, MDCK-f3 cells show regenerated expression and activity ratios of the small GTPases Rac and Rho normally found in untransformed MDCK cells.
Gene_expression (expression) of Rac in MDCK
5) Confidence 0.75 Published 2002 Journal Cancer Res. Section Abstract Doc Link 11912145 Disease Relevance 0.39 Pain Relevance 0.07
In both cell populations we did not observe differences in the expression patterns of COX-2, Bcl-2, Bcl(XL), Bax, and Akt/PKB activity.
Gene_expression (expression) of Akt
6) Confidence 0.75 Published 2001 Journal Exp. Cell Res. Section Abstract Doc Link 11478840 Disease Relevance 0.50 Pain Relevance 0.09
Western blotting analysis demonstrated that the levels of Akt protein and phosphorylated Akt were diminished by the treatment in the control cells, but not in the cells expressing the constitutively active Akt (Fig. 4B).
Gene_expression (expressing) of Akt
7) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.77 Pain Relevance 0
For example, HeLa cells exhibit an abnormal expression pattern of Akt isoforms, in which Akt3 is the most abundant of Akt isoforms (Fig. 1C).
Gene_expression (expression) of Akt in HeLa
8) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.51 Pain Relevance 0
The levels of total Akt mRNA and protein in the SiHa cells were about 2 fold higher than those of HeLa cells (Fig. 6A and data not shown).
Gene_expression (levels) of Akt mRNA in HeLa
9) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0 Pain Relevance 0
Since Akt is a key regulator of cellular survival, we studied the effects of HDAC inhibitors on Akt expression by using quantitative real-time RT-PCR analysis with specific primers and corresponding TaqMan probes for different Akt isoforms.
Gene_expression (expression) of Akt
10) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.64 Pain Relevance 0
In addition, following butyrate treatment the cleaved or activated form of caspase-3 was only observed in the control cells but not in the cells expressing the constitutively active Akt (Fig. 4B).
Gene_expression (expressing) of Akt
11) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.70 Pain Relevance 0
Understanding the molecular basis by which Akt gene expression is regulated will ultimately help us to design better strategies to treat cancer.
Gene_expression (expression) of Akt gene associated with cancer
12) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.27 Pain Relevance 0
Our study demonstrated that HDAC inhibitors, such as valproic acid and butyrate, induce apoptosis in HeLa cervical cancer cells by inhibition of gene expression of Akt1 and Akt2.
Gene_expression (expression) of Akt1 in HeLa associated with cervical cancer and apoptosis
13) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 1.14 Pain Relevance 0
The negative effect of valproic acid or butyrate on Akt expression could be mediated through a direct or indirect mechanism, i.e. through inhibiting deacetylation of nonhistone proteins, such as transcription regulators, or gene activation of some negative regulators of Akt gene transcription.
Gene_expression (expression) of Akt
14) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.45 Pain Relevance 0
Valproic acid treatment also reduced the levels of the Akt1 and Akt2 mRNA, but to a lesser degree (Fig. 1B).
Gene_expression (levels) of Akt1
15) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.33 Pain Relevance 0
We, for the first time, show that the down-regulation of Akt activity is a consequence of inhibition of Akt1 and Akt2 expression by valproic acid and butyrate.
Gene_expression (expression) of Akt1
16) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.65 Pain Relevance 0
Treatment of HeLa cells with HDAC inhibitors such as valproic acid and butyrate leads to inhibition of Akt1 and Akt2 expression, consequently to deactivation of cellular Akt (Fig. 1 and 2).
Gene_expression (expression) of Akt1 in HeLa
17) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.86 Pain Relevance 0
Western blotting analysis demonstrated that the levels of Akt protein and phosphorylated Akt were diminished by the treatment in the control cells, but not in the cells expressing the constitutively active Akt (Fig. 4B).
Gene_expression (levels) of Akt
18) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.80 Pain Relevance 0
Flow cytometry analysis revealed that butyrate was able to induce significant apoptotic death in the control cells but not in the cells expressing the constitutively active Akt (Fig. 4A).
Gene_expression (expressing) of Akt associated with apoptosis and death
19) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.84 Pain Relevance 0
As shown in Fig. 5C, both valproic acid and butyrate decreased the levels of Akt1 and Akt2 mRNA to a certain degree, but not significantly.
Gene_expression (levels) of Akt1
20) Confidence 0.71 Published 2006 Journal Mol Cancer Section Body Doc Link PMC1762018 Disease Relevance 0.25 Pain Relevance 0

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