INT180923

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Context Info
Confidence 0.46
First Reported 2005
Last Reported 2010
Negated 0
Speculated 2
Reported most in Body
Documents 6
Total Number 12
Disease Relevance 7.84
Pain Relevance 2.17

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

peptidase activity (Mmp2) extracellular space (Mmp2) extracellular region (Mmp2)
proteinaceous extracellular matrix (Mmp2) plasma membrane (Mmp2) nucleus (Mmp2)
Anatomy Link Frequency
macrophages 2
endothelial cells 2
plugs 2
alveolar macrophages 2
PC-3 2
Mmp2 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 318 100.00 Very High Very High Very High
Inflammation 18 95.48 Very High Very High Very High
fibrosis 36 72.88 Quite High
alcohol 4 40.16 Quite Low
antagonist 8 35.40 Quite Low
Inflammatory response 3 8.52 Low Low
Potency 18 5.00 Very Low Very Low Very Low
anesthesia 11 5.00 Very Low Very Low Very Low
Pain 7 5.00 Very Low Very Low Very Low
cINOD 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Cancer 1348 99.44 Very High Very High Very High
Metastasis 372 98.60 Very High Very High Very High
Apoptosis 67 97.60 Very High Very High Very High
Cervical Cancer 2 96.80 Very High Very High Very High
Adhesions 2 96.40 Very High Very High Very High
Prostate Cancer 57 95.80 Very High Very High Very High
INFLAMMATION 23 95.48 Very High Very High Very High
Reprotox - General 1 8 88.08 High High
Hypoxia 35 87.36 High High
Sprains And Strains 11 84.44 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This is consistent with another study, mentioned above, in which apocynin, an inhibitor of NADPH oxidase, also inhibited the release of MMP-9 and MMP-2 in SP-D -/- alveolar macrophages [23].
Negative_regulation (inhibited) of Localization (release) of MMP-2 in alveolar macrophages
1) Confidence 0.46 Published 2005 Journal Respir Res Section Body Doc Link PMC548519 Disease Relevance 0.31 Pain Relevance 0.21
Fukaya et al. [18] reported that inhibition of Akt signaling by either the expression of a dominant-negative form of Akt in LM8 cells or the treatment of LM8 cells with LY294002, which is a potent PI3K inhibitor, decreases the secretion of MMP-2 and suppresses cell invasion and motility [18].
Negative_regulation (decreases) of Localization (secretion) of MMP-2
2) Confidence 0.38 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.50 Pain Relevance 0
Inhibition of Akt signaling by TGZ may decrease the secretion of MMP-2, resulting in the decrease of invasiveness and motility in LM8 cells.
Spec (may) Negative_regulation (decrease) of Localization (secretion) of MMP-2
3) Confidence 0.38 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2838820 Disease Relevance 1.02 Pain Relevance 0.03
Taken together, the present findings suggest that inhibition of Akt signaling by TGZ may decrease MMP-2 secretion, thus resulting in the decrease of the invasiveness and motility in LM8 cells.
Spec (may) Negative_regulation (decrease) of Localization (secretion) of MMP-2
4) Confidence 0.38 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.55 Pain Relevance 0
Inhibition of Akt signaling in LM8 cells results in the suppression of the secretion of MMP-2 and the in vitro invasiveness and motility [18].
Negative_regulation (suppression) of Localization (secretion) of MMP-2
5) Confidence 0.37 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.11 Pain Relevance 0
It is possible that the host MMPs did partially compensate (e.g., the reduced growth rate of MMP-2 and MMP-9 null fibroblasts compared to wild-type fibroblasts cocultured with FaDu cells in vivo represents a host compensation for an otherwise more significant effect).
Negative_regulation (reduced) of Localization (rate) of MMP-2 in fibroblasts associated with metalloproteinase
6) Confidence 0.32 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1450297 Disease Relevance 0.65 Pain Relevance 0.38
Gelatin zymography assays indicated that THL dose-dependently inhibited the secretion of MMP-2 and MMP-9 in MDA-MB-231, H1299, PC-3 and CT-26 cancer cells (Fig 2A).
Negative_regulation (inhibited) of Localization (secretion) of MMP-2 in PC-3 associated with cancer and metalloproteinase
7) Confidence 0.20 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2880989 Disease Relevance 0.86 Pain Relevance 0.43
We thus tested whether THL could inhibit the secretion of MMP-2, MMP-9, and uPA in cancer cells.
Negative_regulation (inhibit) of Localization (secretion) of MMP-2 associated with cancer and metalloproteinase
8) Confidence 0.15 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2880989 Disease Relevance 0.90 Pain Relevance 0.39
Moreover, THL inhibited the migration, invasion, and tube formation of endothelial cells in vitro, decreased the secretion of MMP-2 and uPA in endothelial cells, and suppressed neovascularization in Matrigel plugs in mice.
Negative_regulation (decreased) of Localization (secretion) of MMP-2 in plugs associated with metalloproteinase
9) Confidence 0.15 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2880989 Disease Relevance 1.36 Pain Relevance 0.26
We thus tested whether THL could inhibit the secretion of MMP-2 and uPA in endothelial cells.
Negative_regulation (inhibit) of Localization (secretion) of MMP-2 in endothelial cells associated with metalloproteinase
10) Confidence 0.15 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2880989 Disease Relevance 0.14 Pain Relevance 0.22
Zymography assays indicated that THL dose-dependently inhibited the secretion of MMP-2 (Fig 4C) and uPA (Fig 4D) in HMEC-1 cells.
Negative_regulation (inhibited) of Localization (secretion) of MMP-2 associated with metalloproteinase
11) Confidence 0.15 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2880989 Disease Relevance 0.13 Pain Relevance 0.23
Zoledronate as well as alendronate has been found to inhibit secretion and activity of MMP-2 and MMP-9 by tumor cells and tumor-infiltrating macrophages in mouse models of cervical cancer [19] and prostate cancer [50].
Negative_regulation (inhibit) of Localization (secretion) of MMP-2 in macrophages associated with cervical cancer, cancer and prostate cancer
12) Confidence 0.14 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2294135 Disease Relevance 1.31 Pain Relevance 0

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