INT246762

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Context Info
Confidence 0.67
First Reported 2008
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 60
Total Number 60
Disease Relevance 15.71
Pain Relevance 0.25

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

cytosol (Tsc2) signal transduction (Tsc2) Golgi apparatus (Tsc2)
nucleus (Tsc2) intracellular (Tsc2) protein complex (Tsc2)
Anatomy Link Frequency
kidney cortex 6
epithelial cells 2
muscle 1
proximal 1
Tsc2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
adenocard 1 84.72 Quite High
agonist 58 82.24 Quite High
Paracetamol 60 73.16 Quite High
anesthesia 58 53.20 Quite High
cytokine 1 5.00 Very Low Very Low Very Low
cerebral cortex 1 5.00 Very Low Very Low Very Low
transdermal 1 5.00 Very Low Very Low Very Low
Angina 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Tuberous Sclerosis 12 100.00 Very High Very High Very High
Diabetes Mellitus 2262 99.84 Very High Very High Very High
Hyperglycemia 352 99.60 Very High Very High Very High
Injury 232 96.72 Very High Very High Very High
Stress 408 93.84 High High
Body Weight 120 93.00 High High
Apoptosis 129 91.96 High High
Aging 38 77.24 Quite High
Adhesions 58 74.72 Quite High
Death 64 74.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This possibility is given by the fact that Wnt stimulates the mTOR signalling pathway via inhibiting GSK3 phosphorylation of TSC2.
Phosphorylation (phosphorylation) of TSC2
1) Confidence 0.67 Published 2008 Journal Current Genomics Section Body Doc Link PMC2691673 Disease Relevance 0 Pain Relevance 0.04
Interestingly, these data do not appear to predict down-stream Akt signaling since the phosphorylation level of mTOR (Ser2448) [9] (Figure 2A), tuberous sclerosis complex-2 (TSC2) and forkhead box O1 (FoxO1) (data not shown) was lower in the very aged muscle.
Phosphorylation (phosphorylation) of TSC2 in muscle associated with tuberous sclerosis
2) Confidence 0.57 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2712760 Disease Relevance 0.43 Pain Relevance 0.07
Moreover, pretreatment of the cells with NAC inhibited Akt and tuberin phosphorylation and upregulation of OGG1 protein expression in cells exposed to high glucose (Fig. 7D).
Phosphorylation (phosphorylation) of tuberin
3) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
Diabetes is associated with an increase in Akt and tuberin phosphorylation and OGG1 downregulation in the renal cortex.
Phosphorylation (phosphorylation) of tuberin in renal cortex associated with diabetes mellitus
4) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.42 Pain Relevance 0
The fact that oxidant-induced effects on Akt and tuberin phosphorylation correlate well with those of high glucose suggests that ROS may mediate the action of high glucose on Akt, tuberin, and OGG1.
Phosphorylation (phosphorylation) of tuberin
5) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
These data demonstrate that phosphorylation of Akt and tuberin and downregulation of OGG1 are redox sensitive in MCT cells.


Phosphorylation (phosphorylation) of tuberin
6) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
RESULTS—In the renal cortex of diabetic rats, the increase in Akt phosphorylation is associated with enhanced phosphorylation of tuberin, decreased OGG1 protein expression, and 8-oxodG accumulation.
Phosphorylation (phosphorylation) of tuberin in renal cortex associated with diabetes mellitus
7) Confidence 0.35 Published 2008 Journal Diabetes Section Abstract Doc Link PMC2551671 Disease Relevance 0.34 Pain Relevance 0
To confirm the validity of these data obtained in the MCT immortalized cells, we studied the effects of high glucose on the phosphorylation of Akt and tuberin and on OGG1 protein expression in RPTE cells.
Phosphorylation (phosphorylation) of tuberin
8) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
The concept that the PI 3-kinase/Akt pathway regulates tuberin is supported by other observations that the expression of a constitutively active PI 3-kinase or active Akt, including Akt1 or Akt2, induce tuberin phosphorylation (27).
Phosphorylation (phosphorylation) of tuberin
9) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.16 Pain Relevance 0
Hydrogen peroxide induced Akt and tuberin phosphorylation with an effect seen as early as 2.5 min and a peak effect occurring at 5–15 min (Fig. 6A and B), whereas the maximum decrease in OGG1 was observed at 60 min (Fig. 6C).
Phosphorylation (phosphorylation) of tuberin
10) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
Collectively, our data indicate that ROS are signaling molecules responsible for Akt phosphorylation initiated by high glucose leading to tuberin phosphorylation and OGG1 protein downregulation.
Phosphorylation (phosphorylation) of tuberin
11) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.16 Pain Relevance 0
We also investigated the effect of high glucose on tuberin phosphorylation, OGG1 expression, and 8-oxodG accumulations in proximal tubular epithelial cells.
Phosphorylation (phosphorylation) of tuberin in epithelial cells
12) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.40 Pain Relevance 0.09
High glucose caused a rapid increase in Akt and tuberin phosphorylation in a time-dependent manner, with effects that peaked at 2.5–5 min and subsided by 60 min (Fig. 3A and B).
Phosphorylation (phosphorylation) of tuberin
13) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.35 Pain Relevance 0
The correlation between high glucose–induced Akt and tuberin phosphorylation and OGG1 downregulation led us to test the hypothesis that the PI 3-kinase/Akt pathway activated by glucose results in tuberin phosphorylation and OGG1 downregulation.
Phosphorylation (phosphorylation) of tuberin
14) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
These data show that MCT cells are a relevant model and confirm that phosphorylation and inactivation of tuberin via the redox-dependent activation of Akt play a major role in OGG1 downregulation and 8-oxodG accumulation.
Phosphorylation (phosphorylation) of tuberin
15) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.39 Pain Relevance 0
Akt phosphorylation on Ser 473 results in Akt activation, whereas phosphorylation of tuberin on Thr 1,462 results in its inactivation.
Phosphorylation (phosphorylation) of tuberin
16) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.79 Pain Relevance 0
Importantly, we show that ROS, and specifically hydrogen peroxide, directly induce Akt activation and tuberin phosphorylation, resulting in downregulation of OGG1 in MCT cells, indicating that ROS are potential upstream mediators of the effects of high glucose on oxidative DNA damage.
Phosphorylation (phosphorylation) of tuberin
17) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.64 Pain Relevance 0
ROS are required for high glucose–induced Akt and tuberin phosphorylation and OGG1 downregulation in MCT cells.
Phosphorylation (phosphorylation) of tuberin
18) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0 Pain Relevance 0
Phosphorylation of tuberin by Akt affects its function through at least two mechanisms: first, phosphorylation decreases the activity of tuberin; second, phosphorylation destabilizes tuberin by disrupting the complex formation between hamartin and tuberin, resulting in ubiquitination of free tuberin and its degradation by the proteosome (27).
Phosphorylation (Phosphorylation) of tuberin
19) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.06 Pain Relevance 0
The observation that PI 3-kinase and Akt inhibitors block the effect of high glucose on tuberin phosphorylation indicates that the PI 3-kinase/Akt pathway mediates the action of high glucose on tuberin.
Phosphorylation (phosphorylation) of tuberin
20) Confidence 0.35 Published 2008 Journal Diabetes Section Body Doc Link PMC2551671 Disease Relevance 0.46 Pain Relevance 0

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