INT111398

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Context Info
Confidence 0.76
First Reported 2003
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 37
Total Number 37
Disease Relevance 23.78
Pain Relevance 7.17

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
cartilage 2
PC-3 2
macrophages 1
alveolar macrophages 1
fibroblasts 1
Mmp2 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 748 100.00 Very High Very High Very High
fibrosis 182 98.00 Very High Very High Very High
Inflammatory response 23 97.64 Very High Very High Very High
Morphine 3 97.12 Very High Very High Very High
Inflammation 163 95.16 Very High Very High Very High
Osteoarthritis 42 91.92 High High
Chronic pancreatitis 10 89.00 High High
Snapping jaw 8 88.08 High High
interstitial cystitis 1 84.48 Quite High
chemokine 2 79.96 Quite High
Disease Link Frequency Relevance Heat
Fibrosis 123 99.84 Very High Very High Very High
Reprotox - General 1 24 99.64 Very High Very High Very High
Pancreatic Cancer 26 99.50 Very High Very High Very High
Cancer 2542 99.48 Very High Very High Very High
Fibrosarcoma 7 99.48 Very High Very High Very High
Pulmonary Fibrosis 90 98.40 Very High Very High Very High
Metastasis 768 98.12 Very High Very High Very High
INFLAMMATION 196 97.46 Very High Very High Very High
Apoptosis 126 97.28 Very High Very High Very High
Colon Cancer 67 97.20 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Gelatinase activities and immunohistochemical localization of MMP-2, -3, -8, -9, and -13 and TIMP-1 and -2 were examined in mandibular condyle cartilage of neonatal mice up to 18 months old.
Localization (localization) of MMP-2 in cartilage
1) Confidence 0.76 Published 2003 Journal Histochem. Cell Biol. Section Abstract Doc Link 12827373 Disease Relevance 0.86 Pain Relevance 0.56
Gelatinase activities and immunohistochemical localization of MMP-2, -3, -8, -9, and -13 and TIMP-1 and -2 were examined in mandibular condyle cartilage of neonatal mice up to 18 months old.
Localization (localization) of Gelatinase in cartilage
2) Confidence 0.71 Published 2003 Journal Histochem. Cell Biol. Section Abstract Doc Link 12827373 Disease Relevance 0.87 Pain Relevance 0.56
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.
Localization (secretion) of MMP-2
3) Confidence 0.70 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.55 Pain Relevance 0
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].
Localization (secretion) of MMP-2
4) Confidence 0.70 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.50 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].
Localization (secretion) of MMP-2
5) Confidence 0.70 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.11 Pain Relevance 0
Effect of TGZ on cell invasion, cell motility, and MMP-2 secretion
Localization (secretion) of MMP-2
6) Confidence 0.70 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.19 Pain Relevance 0.03
In rodents, MMP-2, MMP-3, MMP-9, MMP-13, MMP-14, as well as TIMP-1 and TIMP-2 are expressed in early stages of HSC activation and have been implicated in fibrogenesis as well as fibrolysis (reviewed in [20]).
Localization (implicated) of MMP-2 associated with fibrosis
7) Confidence 0.68 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2892485 Disease Relevance 0.90 Pain Relevance 0.31
Our results indicated that several genes known to be part of the inflammatory response were found downstream of PAR1 activation (b2m, ccl7, cd200, cd63, cdbpd, cfl1, dusp1, fkbp1a, fth1, hspb1, marcksl1, mmp2, myo5a, nfkbia, pax1, plaur, ppia, ptpn1, ptprcap, s100a10, sim2, and tnfaip2).
Localization (ppia) of mmp2 associated with inflammatory response
8) Confidence 0.67 Published 2007 Journal BMC Physiol Section Body Doc Link PMC1853107 Disease Relevance 0.82 Pain Relevance 0.32
Matrix metalloproteinase 2 secretion in WEHI 164 fibrosarcoma cells is nitric oxide-related and modified by morphine.
Localization (secretion) of metalloproteinase 2 in WEHI 164 associated with fibrosarcoma, metalloproteinase and morphine
9) Confidence 0.63 Published 2006 Journal Eur. J. Pharmacol. Section Title Doc Link 16386243 Disease Relevance 0.69 Pain Relevance 0.65
One possible explanation is that the increased release of MMP-2 in the inner lung parenchyma may result from downstream events caused by phagocyte activation and ROS production during inflammation.
Localization (release) of MMP-2 in parenchyma associated with inflammation
10) Confidence 0.62 Published 2005 Journal Respir Res Section Body Doc Link PMC548519 Disease Relevance 0.31 Pain Relevance 0.14
MMP induction, assessed by gelatinase release, has been reported in various cases of pulmonary fibrosis in human and experimental models [13,25,26].
Localization (release) of gelatinase associated with fibrosis and pulmonary fibrosis
11) Confidence 0.62 Published 2005 Journal Respir Res Section Body Doc Link PMC548519 Disease Relevance 0.49 Pain Relevance 0.21
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].
Localization (release) of MMP-2 in alveolar macrophages
12) Confidence 0.62 Published 2005 Journal Respir Res Section Body Doc Link PMC548519 Disease Relevance 0.31 Pain Relevance 0.21
The activity of MMP-2 secreted by TGZ-treated cells was lower than that secreted by untreated cells.
Localization (secreted) of MMP-2
13) Confidence 0.61 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2838820 Disease Relevance 0.99 Pain Relevance 0.04
LM8 cells in both the untreated and TGZ-treated cultures secreted MMP-2; however, the activity of MMP-2 secreted from TGZ-treated cells was 46% of that secreted from untreated cells (p < 0.01).


Localization (secreted) of MMP-2
14) Confidence 0.61 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0 Pain Relevance 0
The activity of MMP-2 secreted by TGZ-treated cells was lower than that secreted by untreated cells.
Localization (secreted) of MMP-2
15) Confidence 0.61 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2838820 Disease Relevance 1.06 Pain Relevance 0.04
Inhibition of Akt signaling by TGZ may decrease the secretion of MMP-2, resulting in the decrease of invasiveness and motility in LM8 cells.
Localization (secretion) of MMP-2
16) Confidence 0.61 Published 2010 Journal BMC Cancer Section Abstract Doc Link PMC2838820 Disease Relevance 1.02 Pain Relevance 0.03
The activity of MMP-2 secreted into conditioned media during the last 24 h of the 3-day treatment period was assayed by gelatin zymography (Figure 3C).
Localization (secreted) of MMP-2
17) Confidence 0.61 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.12 Pain Relevance 0
In the present study, we found that TGZ-treated LM8 cells were less invasive and less motile (Figure 3A and 3B) and exhibited lower secretion of MMP-2 compared with untreated cells (Figure 3C).
Localization (secretion) of MMP-2
18) Confidence 0.61 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.55 Pain Relevance 0.03
The several lines of evidence reveal that Akt, which functions downstream of PI3K, is associated with the invasiveness and motility of tumor cells [18,30-32] and the secretion of MMP-2 [18,33,34].
Localization (secretion) of MMP-2 associated with cancer
19) Confidence 0.57 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0.54 Pain Relevance 0
Indeed, with increasing complexity of the model system, the importance of MMP-2 and MMP-9 became apparent.
Localization (importance) of MMP-2 associated with metalloproteinase
20) Confidence 0.56 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1450297 Disease Relevance 0.90 Pain Relevance 0.56

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