INT34485

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Context Info
Confidence 0.50
First Reported 1987
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 17
Total Number 21
Disease Relevance 9.96
Pain Relevance 10.49

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
monocytes 3
fibroblasts 3
chondrocytes 2
MMP2 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 832 100.00 Very High Very High Very High
rheumatoid arthritis 228 100.00 Very High Very High Very High
Morphine 24 100.00 Very High Very High Very High
tetrodotoxin 6 99.60 Very High Very High Very High
Cannabinoid receptor 18 99.50 Very High Very High Very High
opiate 3 98.96 Very High Very High Very High
antagonist 29 98.32 Very High Very High Very High
Kinase C 3 98.00 Very High Very High Very High
narcan 9 97.88 Very High Very High Very High
COX-2 inhibitor 135 97.04 Very High Very High Very High
Disease Link Frequency Relevance Heat
Adhesions 230 100.00 Very High Very High Very High
Rheumatoid Arthritis 228 100.00 Very High Very High Very High
Primary Sclerosing Cholangitis 44 100.00 Very High Very High Very High
Infection 520 99.36 Very High Very High Very High
Colon Cancer 9 97.36 Very High Very High Very High
Stress 1 96.76 Very High Very High Very High
Lung Cancer 5 96.64 Very High Very High Very High
Prostate Cancer 3 95.68 Very High Very High Very High
Glioma 12 94.56 High High
Herpes Simplex Virus 1190 92.16 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
It also lowered down the activity of MMP-2 and MMP-9, and could reduce of MMP-2 secretion of cell lines.
Negative_regulation (reduce) of Localization (secretion) of MMP-2
1) Confidence 0.50 Published 2005 Journal J. Neurooncol. Section Abstract Doc Link 15803368 Disease Relevance 0.26 Pain Relevance 0
NS398 also reduced the amount of MMP-2, not MMP-9, released into the medium.
Negative_regulation (reduced) of Localization (released) of MMP-2
2) Confidence 0.40 Published 2001 Journal FEBS Lett. Section Abstract Doc Link 11728453 Disease Relevance 0.41 Pain Relevance 0.30
MMP-2 activity assay showed the total and active MMP-2 secretion was suppressed by 500 microM/ml of indomethacin.
Negative_regulation (suppressed) of Localization (secretion) of MMP-2
3) Confidence 0.37 Published 2005 Journal J. Neurooncol. Section Abstract Doc Link 15803368 Disease Relevance 0.36 Pain Relevance 0.14
With immune complexes, there was only modest inhibition of gelatinase release by any of the drugs at 250-1000 microM.
Negative_regulation (inhibition) of Localization (release) of gelatinase
4) Confidence 0.34 Published 1987 Journal Biochem. Pharmacol. Section Abstract Doc Link 3038127 Disease Relevance 0.17 Pain Relevance 0.17
The pro-MMP-9, MMP-9 and MMP-2 secretion in the co-culture of differentiated THP-1 cells and fibroblasts decreased significantly (27.5 ± 12.7%, 25.4 ± 12.4% and 25.5 ± 3.8%, respectively) in the AP9 group compared with those without AP9 (p < 0.01; Fig. 5d).
Negative_regulation (decreased) of Localization (secretion) of MMP-2 in fibroblasts associated with metalloproteinase
5) Confidence 0.26 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.40 Pain Relevance 0.59
By exploiting the cartilage explant culture, p-hydroxycinnamaldehyde suppressed loss of uronic acid, resulting in release of hyaluronan (HA), sulfated glycosaminoglycans (s-GAGs) and matrix metalloproteinases (MMPs). p-Hydroxycinnamaldehyde and interleukin-1beta (IL-1beta), when incubated in primary human chondrocytes, also reduced release of HA, s-GAG and MMP-2.
Negative_regulation (reduced) of Localization (release) of MMP-2 in chondrocytes associated with metalloproteinase
6) Confidence 0.24 Published 2009 Journal Phytochemistry Section Abstract Doc Link 19118849 Disease Relevance 0.29 Pain Relevance 0.35
Concomitantly, cannabinoid receptor activation specifically decreased invasiveness of PSC, MMP-2 secretion and led to changes in PSC phenotype accompanied by a reduction of intracellular stress fibres.


Negative_regulation (decreased) of Localization (secretion) of MMP-2 associated with stress, cannabinoid receptor and primary sclerosing cholangitis
7) Confidence 0.22 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2253501 Disease Relevance 1.18 Pain Relevance 0.98
RESULTS: Gelatin zymography showed that all NSAIDs generally decreased MMP-2 secretion in chondral, meniscal and synovial cultures as well as MMP-9 production in meniscal and synovial cultures.
Negative_regulation (decreased) of Localization (secretion) of MMP-2
8) Confidence 0.22 Published 2008 Journal Clin. Biochem. Section Body Doc Link 17996201 Disease Relevance 0.09 Pain Relevance 0
NS-398 pretreatrment decreased the secretion of total MMP-2 but not that of active MMP-2 (Figure 9E).
Negative_regulation (decreased) of Localization (secretion) of MMP-2 associated with metalloproteinase
9) Confidence 0.20 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 0.34 Pain Relevance 0.76
AP9 had some inhibitory effect on the secretion of pro-MMP9 (control, 33.7 ± 18.5%; RA, 31.8 ± 16.2), MMP-9 (control, 41.9 ± 5.8%; RA, 43.8 ± 5.1%) and MMP-2 (control, 100%; RA, 63.9 ± 6.2%) in the co-culture of human monocytes and fibroblasts in both the normal control and RA groups (Fig. 4c).
Negative_regulation (effect) of Localization (secretion) of MMP-2 in monocytes associated with metalloproteinase and rheumatoid arthritis
10) Confidence 0.19 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.45 Pain Relevance 0.61
TIVE-LTC cells secreted diminished levels of MMP-2 when compared to de novo infected cells (Figure 9E and 9G), therefore COX-2 inhibition could not effectively down-regulate active MMP-2 secretion during de novo infection (Figure 9E and 9F) compared to TIVE-LTC cells.
Negative_regulation (diminished) of Localization (secreted) of MMP-2 associated with metalloproteinase and infection
11) Confidence 0.17 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 1.24 Pain Relevance 0.61
NS-398 pretreatrment decreased the secretion of total MMP-2 but not that of active MMP-2 (Figure 9E).
Negative_regulation (decreased) of Localization (secretion) of MMP-2 associated with metalloproteinase
12) Confidence 0.17 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 0.35 Pain Relevance 0.76
TIVE-LTC cells secreted diminished levels of MMP-2 when compared to de novo infected cells (Figure 9E and 9G), therefore COX-2 inhibition could not effectively down-regulate active MMP-2 secretion during de novo infection (Figure 9E and 9F) compared to TIVE-LTC cells.
Negative_regulation (regulate) of Localization (secretion) of MMP-2 associated with metalloproteinase and infection
13) Confidence 0.15 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 1.11 Pain Relevance 0.64
TIVE-LTC cells secreted diminished levels of MMP-2 when compared to de novo infected cells (Figure 9E and 9G), therefore COX-2 inhibition could not effectively down-regulate active MMP-2 secretion during de novo infection (Figure 9E and 9F) compared to TIVE-LTC cells.
Neg (not) Negative_regulation (down) of Localization (secretion) of MMP-2 associated with metalloproteinase and infection
14) Confidence 0.15 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 1.11 Pain Relevance 0.64
M NS-398, reported a reduction in the release of pro and active MMP-2 and MMP-9 in the culture media [15,38].
Negative_regulation (reduction) of Localization (release) of MMP-2 associated with metalloproteinase
15) Confidence 0.09 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1559713 Disease Relevance 0.28 Pain Relevance 0.41
TTX also significantly reduced the secretion of matrix metalloproteinase-2 6 and 12 h after the treatment (P < 0.01 and P < 0.05, respectively).
Negative_regulation (reduced) of Localization (secretion) of matrix metalloproteinase-2 6 associated with tetrodotoxin and metalloproteinase
16) Confidence 0.08 Published 2009 Journal Am. J. Physiol. Heart Circ. Physiol. Section Abstract Doc Link 18978189 Disease Relevance 0.14 Pain Relevance 0.62
AP9 had some inhibitory effect on the secretion of pro-MMP9 (control, 33.7 ± 18.5%; RA, 31.8 ± 16.2), MMP-9 (control, 41.9 ± 5.8%; RA, 43.8 ± 5.1%) and MMP-2 (control, 100%; RA, 63.9 ± 6.2%) in the co-culture of human monocytes and fibroblasts in both the normal control and RA groups (Fig. 4c).
Negative_regulation (effect) of in fibroblasts Localization (secretion) of MMP-2 in monocytes associated with metalloproteinase and rheumatoid arthritis
17) Confidence 0.07 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.45 Pain Relevance 0.61
Further, 10 microM morphine also blocks indolactam V-induced homotypic aggregation and gelatinase secretion.
Negative_regulation (blocks) of Localization (secretion) of gelatinase associated with morphine
18) Confidence 0.03 Published 2001 Journal J. Cell. Physiol. Section Abstract Doc Link 11598903 Disease Relevance 0.49 Pain Relevance 0.98
The inhibitory effect of morphine on cell-matrix adhesion and gelatinase secretion was not inhibited by the opiate receptor antagonist naloxone (1 microM).
Negative_regulation (effect) of Localization (secretion) of gelatinase associated with antagonist, narcan, opiate, adhesions and morphine
19) Confidence 0.03 Published 2001 Journal J. Cell. Physiol. Section Abstract Doc Link 11598903 Disease Relevance 0.49 Pain Relevance 0.98
Morphine inhibits indolactam V-induced U937 cell adhesion and gelatinase secretion.
Negative_regulation (inhibits) of Localization (secretion) of gelatinase associated with adhesions and morphine
20) Confidence 0.03 Published 2001 Journal J. Cell. Physiol. Section Title Doc Link 11598903 Disease Relevance 0.31 Pain Relevance 0.36

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