INT116110

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Context Info
Confidence 0.66
First Reported 2004
Last Reported 2011
Negated 0
Speculated 1
Reported most in Body
Documents 20
Total Number 21
Disease Relevance 10.53
Pain Relevance 1.64

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

extracellular matrix organization (PTK2) embryo development (PTK2) microtubule organizing center (PTK2)
cytoplasm (PTK2) signal transducer activity (PTK2) cytosol (PTK2)
Anatomy Link Frequency
AsPC-1 2
myometrium 1
Section 3 1
BxPC-3 1
epithelial cells 1
PTK2 (Homo sapiens)
Pain Link Frequency Relevance Heat
Kappa opioid receptor 8 99.92 Very High Very High Very High
qutenza 11 98.68 Very High Very High Very High
antagonist 38 97.94 Very High Very High Very High
Opioid 3 97.72 Very High Very High Very High
agonist 13 95.60 Very High Very High Very High
metalloproteinase 57 90.32 High High
chemokine 6 79.24 Quite High
cytokine 8 74.16 Quite High
Inflammation 14 59.92 Quite High
Pain 6 56.32 Quite High
Disease Link Frequency Relevance Heat
Adhesions 368 100.00 Very High Very High Very High
Pancreatic Cancer 412 99.58 Very High Very High Very High
Malignant Neoplastic Disease 19 98.80 Very High Very High Very High
Breast Cancer 138 98.78 Very High Very High Very High
Cancer 633 98.20 Very High Very High Very High
Apoptosis 386 97.88 Very High Very High Very High
Retinoblastoma 1 95.32 Very High Very High Very High
Skin Cancer 21 94.12 High High
Wound Healing 2 88.40 High High
Reprotox - General 3 8 79.04 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Previous study in breast cancer cells has also found that FRNK overexpression inhibited the activation of FAK and PKB and thus enhanced chemotherapy-induced cell apoptosis [37].
Positive_regulation (activation) of FAK associated with breast cancer and apoptosis
1) Confidence 0.66 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.59 Pain Relevance 0
Treatment with the opioid antagonist alpha(s1) casomorphin resulted in rapid and potent actin remodeling in A375 cells, regulated by rapid activation of the FAK/PI-3K/Rac1 signaling.
Positive_regulation (activation) of FAK in A375 associated with antagonist and opioid
2) Confidence 0.54 Published 2007 Journal Cell. Physiol. Biochem. Section Abstract Doc Link 17982280 Disease Relevance 0.33 Pain Relevance 0.15
A low level of constitutively activated FAK and Akt was found in AsPC-1 cells, and a rapid and strong stimulation of FAK and Akt phosphorylation was induced by LN.
Positive_regulation (activated) of FAK in AsPC-1
3) Confidence 0.48 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.22 Pain Relevance 0
These results indicated that in AsPC-1 cells, LN induced FAK and Akt phosphorylation in a time-dependent manner, and LN-induced Akt phosphorylation was mediated by FAK activation.


Positive_regulation (activation) of FAK in AsPC-1
4) Confidence 0.44 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.28 Pain Relevance 0
Phosphorylation at Tyr397 correlates with increased catalytic activity of FAK and is important for tyrosine phosphorylation of focal-adhesion-associated proteins [35,36].
Positive_regulation (increased) of FAK associated with adhesions
5) Confidence 0.44 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.55 Pain Relevance 0
It specifically blocks FAK phosphorylation and thus targets FAK catalytic activity.
Positive_regulation (targets) of FAK
6) Confidence 0.44 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.41 Pain Relevance 0
These studies demonstrate that the activation of JNK by kappa-opioid receptors is routed via Gbetagamma, Src, FAK, Sos, Rac, and Cdc42.
Positive_regulation (routed) of FAK associated with kappa opioid receptor
7) Confidence 0.44 Published 2004 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 14996948 Disease Relevance 0.16 Pain Relevance 0.27
We demonstrated herein that specific RNAi against FAK reduced FAK expression, decreased FAK phosphorylation and thus suppressed the intrinsic chemoresistance to Gem in Panc-1 cells, which had a high level of pFAK (pY397).
Positive_regulation (level) of pFAK
8) Confidence 0.42 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.57 Pain Relevance 0
In our study, we used the two kinds of plasmids (FAK RNAi plasmid and FRNK overexpression plasmid) to further dissect the role of constitutive FAK phosphorylation in the chemoresistance of pancreatic cancer cells that had high level of pFAK.
Positive_regulation (level) of pFAK associated with pancreatic cancer
9) Confidence 0.42 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.75 Pain Relevance 0
Panc-1 displayed a relatively high level of pFAK (pY397), while MiaPaCa-2 and BxPC-3 cells displayed moderate levels.
Positive_regulation (level) of pFAK in BxPC-3
10) Confidence 0.39 Published 2009 Journal Mol Cancer Section Body Doc Link PMC2806309 Disease Relevance 0.38 Pain Relevance 0
We have recently identified a specific signaling pathway that regulates actin reorganization in malignant human breast and prostate epithelial cells associated with FAK, PI-3K and Rac1 activation.
Positive_regulation (activation) of FAK in epithelial cells associated with malignant neoplastic disease
11) Confidence 0.36 Published 2007 Journal Cell. Physiol. Biochem. Section Abstract Doc Link 17982280 Disease Relevance 0.23 Pain Relevance 0.09
By using phosphotyrosine screening and mass spectrometry of stretched human myometrial samples, we identify 3 stretch-activated focal adhesion proteins, FAK, p130Cas, and alpha actinin.
Positive_regulation (activated) of FAK associated with adhesions
12) Confidence 0.18 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2759504 Disease Relevance 0.43 Pain Relevance 0
However, acute stretch did cause a significant increase in FAK-Y925 phosphorylation (Fig. 5A, bottom) perhaps mimicking events that occur later in vivo during the switch to initiate labor.
Positive_regulation (increase) of FAK
13) Confidence 0.17 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2759504 Disease Relevance 0.21 Pain Relevance 0
FAK-Y397, which signals integrin engagement, is constitutively phosphorylated in term human myometrium whereas FAK-Y925, which signals downstream ERK activation, is phosphorylated during stretch.
Positive_regulation (activation) of FAK in myometrium
14) Confidence 0.17 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2759504 Disease Relevance 0.50 Pain Relevance 0
At this time, it is unclear whether the activation of Smad1 and FAK are due to genistein’s inhibition of MEK4 or via a different signaling mechanism
Spec (whether) Positive_regulation (activation) of FAK
15) Confidence 0.17 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 0.51 Pain Relevance 0
Genistein consistently inhibits FAK activation in all of these studies, irrespective of its effect upon adhesion [120, 123, 125].
Positive_regulation (activation) of FAK associated with adhesions
16) Confidence 0.17 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 1.36 Pain Relevance 0
Signaling experiments show that capsaicin inhibits VEGF-induced p38 mitogen-activated protein kinase, p125(FAK), and AKT activation, but its molecular target is distinct from the VEGF receptor KDR/Flk-1.
Positive_regulation (activation) of FAK associated with qutenza
17) Confidence 0.14 Published 2004 Journal Cancer Res. Section Abstract Doc Link 14744780 Disease Relevance 0.29 Pain Relevance 0.81
These results imply that genistein’s effects on both cell adhesion (see Section 3.2) and cell migration are in part regulated by its ability to inhibit activation of FAK.
Positive_regulation (activation) of FAK in Section 3 associated with adhesions
18) Confidence 0.12 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 0.55 Pain Relevance 0.18
Additionally, genistein inhibits FAK activation, resulting in increased cell adhesion.
Positive_regulation (activation) of FAK associated with adhesions
19) Confidence 0.11 Published 2010 Journal Cancer Metastasis Rev Section Body Doc Link PMC2933845 Disease Relevance 0.49 Pain Relevance 0
VEGF also regulated focal adhesion assembly in HBMECs through activation of FAK and RAFTK/Pyk2 [45].
Positive_regulation (activation) of FAK associated with adhesions
20) Confidence 0.11 Published 2011 Journal Pathology Research International Section Body Doc Link PMC3021881 Disease Relevance 1.39 Pain Relevance 0.08

General Comments

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