INT120403

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Context Info
Confidence 0.60
First Reported 2004
Last Reported 2010
Negated 2
Speculated 1
Reported most in Body
Documents 2
Total Number 19
Disease Relevance 1.92
Pain Relevance 0.50

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

plasma membrane (EPHB2)
Anatomy Link Frequency
L929 8
EPHB2 (Homo sapiens)
Pain Link Frequency Relevance Heat
bradykinin 12 100.00 Very High Very High Very High
Kinase C 108 80.40 Quite High
b2 receptor 3 75.00 Quite High
Pain 1 47.92 Quite Low
Inflammation 1 45.04 Quite Low
Migraine 18 5.00 Very Low Very Low Very Low
Neuropathic pain 18 5.00 Very Low Very Low Very Low
Immobilon 18 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 216 94.36 High High
Glioma 108 90.88 High High
Neuroblastoma 18 76.64 Quite High
Adenocarcinoma 36 73.52 Quite High
Epilepsy 36 70.44 Quite High
Breast Cancer 1 59.84 Quite High
Malignant Neoplastic Disease 1 55.88 Quite High
Pressure And Volume Under Development 1 48.40 Quite Low
Pain 1 47.92 Quite Low
Increased Venous Pressure Under Development 1 47.68 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These results demonstrate that exposure to VPA reversed the effects of caRas expression on L929 cell morphology and the degree of Erk1/2 phosphorylation.
Regulation (effects) of Phosphorylation (phosphorylation) of Erk1 in L929
1) Confidence 0.60 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
The effects of BK on proliferation, ERK1/2 phosphorylation, and c-Fos expression were abolished by GF109203X, which inhibits PKC-delta isozyme.
Regulation (effects) of Phosphorylation (phosphorylation) of ERK associated with bradykinin
2) Confidence 0.44 Published 2004 Journal J. Cell. Physiol. Section Abstract Doc Link 15281091 Disease Relevance 0.12 Pain Relevance 0.40
Therefore, we hypothesize that the modulation of the degree of Erk1/2 phosphorylation by VPA is of central importance for drug-mediated inhibition of cell inhibition.
Regulation (modulation) of Phosphorylation (phosphorylation) of Erk1
3) Confidence 0.44 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
As expected, VPA increased the degree of Erk1/2 phosphorylation compared with untreated cells (Figure 5g, lanes 1 and 3).
Regulation (degree) of Phosphorylation (phosphorylation) of Erk1
4) Confidence 0.44 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
The immunoblot presented in Figure 5b shows that L929 cells expressing caRas exhibited higher degrees of Erk1/2 phosphorylation than control-transfected cells when grown in the absence of VPA (Figure 5b, lanes 2 and 1).
Regulation (control) of Phosphorylation (phosphorylation) of Erk1 in L929
5) Confidence 0.44 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
In conclusion, VPA has highly cell type-specific effects on the degree of HDAC inhibition and on changes in the degree of Erk1/2 phosphorylation.
Regulation (changes) of Phosphorylation (phosphorylation) of Erk1
6) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Furthermore, no apparent relationship was observed between the effects of VPA on HDAC inhibition and cell growth, whereas VPA was likely to affect the growth of a given cell type if it affected the degree of Erk1/2 phosphorylation in that cell type at physiologically relevant concentrations.


Regulation (affected) of Phosphorylation (phosphorylation) of Erk1
7) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Figure 3c and 3e show time-response effects of VPA on the degree of Erk1/2 phosphorylation.
Regulation (effects) of Phosphorylation (phosphorylation) of Erk1
8) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
However, cell lines demonstrating significant changes in the degree of Erk1/2 phosphorylation in response to VPA, generally had lower IC50 values for growth than cell lines with unaffected degrees of Erk1/2 phosphorylation (pERK-change, p < 0.05 and growth IC50 >3 mM, 0 cell lines; pERK-change, p < 0.05 and growth IC50 <3 mM, 5 cell lines; pERK-change, p > 0.05 and growth IC50 <3 mM, 4 cell lines; pERK-change, p > 0.05 and growth IC50 >3 mM, 1 cell line; p < 0.05; ?
Regulation (changes) of Phosphorylation (phosphorylation) of Erk1
9) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Moreover, we found that the effect of VPA on the degree of Erk1/2 phosphorylation was highly cell type-specific.
Regulation (effect) of Phosphorylation (phosphorylation) of Erk1
10) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0.18 Pain Relevance 0
These results suggest that VPA can modulate the degree of Erk1/2 phosphorylation in a manner unrelated to HDAC inhibition and emphasize that changes in the degree of Erk1/2 phosphorylation are also important for the anti-cancer properties of VPA.



Regulation (modulate) of Phosphorylation (phosphorylation) of Erk1 associated with cancer
11) Confidence 0.26 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2918577 Disease Relevance 0.29 Pain Relevance 0
Therefore, a potential relationship between the effects of VPA on the degree of Erk1/2 phosphorylation and cell motility was investigated further in L929 cells.
Regulation (effects) of Phosphorylation (phosphorylation) of Erk1 in L929
12) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
Importantly, no relationship was found between the effects of VPA on HDAC inhibition and changes in the degree of Erk1/2 phosphorylation, cell growth, or motility.
Regulation (changes) of Phosphorylation (phosphorylation) of Erk1
13) Confidence 0.26 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2918577 Disease Relevance 0.22 Pain Relevance 0
In contrast, modulation of cell growth and motility was in some cell lines related to changes in the degree of Erk1/2 phosphorylation, which was regulated at the level of Raf.


Regulation (regulated) of Phosphorylation (phosphorylation) of Erk1
14) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0.46 Pain Relevance 0.03
In contrast, modulation of cell growth and motility was in some cell lines related to changes in the degree of Erk1/2 phosphorylation, which was regulated at the level of Raf.


Regulation (changes) of Phosphorylation (phosphorylation) of Erk1
15) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0.45 Pain Relevance 0.03
However, cell lines demonstrating significant changes in the degree of Erk1/2 phosphorylation in response to VPA, generally had lower IC50 values for growth than cell lines with unaffected degrees of Erk1/2 phosphorylation (pERK-change, p < 0.05 and growth IC50 >3 mM, 0 cell lines; pERK-change, p < 0.05 and growth IC50 <3 mM, 5 cell lines; pERK-change, p > 0.05 and growth IC50 <3 mM, 4 cell lines; pERK-change, p > 0.05 and growth IC50 >3 mM, 1 cell line; p < 0.05; ?
Neg (unaffected) Regulation (unaffected) of Phosphorylation (phosphorylation) of Erk1
16) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
However, no apparent relationship was found between the expression of the respective Raf isoforms and the observed changes in the degree of Erk1/2 phosphorylation in response to VPA.
Spec (observed) Regulation (changes) of Phosphorylation (phosphorylation) of Erk1
17) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0.21 Pain Relevance 0.04
Effects of VPA on individual cell motility and the degree of Erk1/2 phosphorylation in L929 cells
Regulation (Effects) of Phosphorylation (phosphorylation) of Erk1 in L929
18) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0
However, four of the five cell lines that did not demonstrate significant changes in the degree of Erk1/2 phosphorylation in response to VPA (Figure 1b) did not have IC50 values for growth within the tested concentration range (below 3 mM; Table 1), whereas all five cell lines demonstrating significant changes in the degree of Erk1/2 phosphorylation in response to VPA had IC50 values for growth below 3 mM.
Neg (not) Regulation (changes) of Phosphorylation (phosphorylation) of Erk1
19) Confidence 0.26 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2918577 Disease Relevance 0 Pain Relevance 0

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