INT86295

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Context Info
Confidence 0.76
First Reported 2000
Last Reported 2010
Negated 5
Speculated 7
Reported most in Body
Documents 114
Total Number 121
Disease Relevance 73.68
Pain Relevance 24.25

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
lung 7
fibroblasts 5
endothelial cells 4
extracellular matrix 3
uterus 2
Mmp2 (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 1645 100.00 Very High Very High Very High
COX2 1 100.00 Very High Very High Very High
Inflammation 786 99.84 Very High Very High Very High
rheumatoid arthritis 317 99.84 Very High Very High Very High
Dismenorea 12 99.84 Very High Very High Very High
cINOD 92 99.80 Very High Very High Very High
Central nervous system 19 99.48 Very High Very High Very High
Chronic pancreatitis 6 99.20 Very High Very High Very High
cytokine 287 98.98 Very High Very High Very High
palliative 310 98.84 Very High Very High Very High
Disease Link Frequency Relevance Heat
Adhesions 261 100.00 Very High Very High Very High
Metastasis 1392 99.96 Very High Very High Very High
Osteogenic Sarcomas 239 99.96 Very High Very High Very High
Cancer 4630 99.86 Very High Very High Very High
INFLAMMATION 965 99.84 Very High Very High Very High
Rheumatoid Arthritis 397 99.84 Very High Very High Very High
Dysmenorrhea 12 99.84 Very High Very High Very High
Repression 3 99.80 Very High Very High Very High
Fibrosis 181 99.64 Very High Very High Very High
Fibrosarcoma 13 99.58 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, only the former maintained high levels of expression of a 90 kD gelatinase up to at least 96 h post ET injection, while in the latter gelatinase expression was down regulated by 24 h.
Gene_expression (expression) of gelatinase
1) Confidence 0.76 Published 2000 Journal Pain Section Abstract Doc Link 10666546 Disease Relevance 0.75 Pain Relevance 0.78
Palliative resection enhances MMP2 activity, elevates tumor protein levels of MMP2 and VEGF, and down-regulates TIMP2 in situ
Gene_expression (levels) of MMP2 associated with cancer and palliative
2) Confidence 0.72 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.60 Pain Relevance 0.59
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]).
Gene_expression (expressed) of MMP-2 associated with fibrosis
3) Confidence 0.70 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2892485 Disease Relevance 0.89 Pain Relevance 0.31
Using the mouse fibrosarcoma cell line WEHI 164, producing high amounts of MMP-2, we investigated whether we could modulate its production.
Gene_expression (producing) of MMP-2 in WEHI 164 associated with fibrosarcoma and metalloproteinase
4) Confidence 0.70 Published 2006 Journal Eur. J. Pharmacol. Section Abstract Doc Link 16386243 Disease Relevance 0.73 Pain Relevance 0.67
Effect of TGZ on the expression and activity of MMP-2 within tumors
Gene_expression (expression) of MMP-2 associated with cancer
5) Confidence 0.68 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 1.46 Pain Relevance 0
The LM8 cell line, which was established from Dunn murine osteosarcoma, expresses MMP-2 and VEGF, possesses an extremely high metastatic potency, and has been used as an excellent tool for the study of inhibitory agents against pulmonary metastasis [16].
Gene_expression (expresses) of MMP-2 associated with osteogenic sarcomas, metastasis and potency
6) Confidence 0.68 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 1.42 Pain Relevance 0.18
These findings suggest that the TGZ-induced inhibition of MMP-2 expression within the tumor may prevent the local invasion at the primary site, thus resulting in the suppression of the development of metastasis in the lung.
Gene_expression (expression) of MMP-2 in lung associated with cancer and metastasis
7) Confidence 0.68 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 1.18 Pain Relevance 0
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).
Gene_expression (cdbpd) of mmp2 associated with inflammatory response
8) Confidence 0.61 Published 2007 Journal BMC Physiol Section Body Doc Link PMC1853107 Disease Relevance 0.87 Pain Relevance 0.35
While MMP-9 is released primarily by inflammatory cells, MMP-2 is synthesized by structural cells including fibroblasts and endothelial and epithelial cells.
Gene_expression (synthesized) of MMP-2 in epithelial cells associated with inflammation
9) Confidence 0.60 Published 2005 Journal Respir Res Section Body Doc Link PMC548519 Disease Relevance 0.58 Pain Relevance 0.46
MMP-9 levels were highly correlated with neutrophil infiltration, while MMP-2 is known to be produced mainly by epithelial [27] and mesenchymal cells, such as fibroblasts, which are involved in collagen production and deposition [9,25].
Gene_expression (produced) of MMP-2 in fibroblasts
10) Confidence 0.60 Published 2005 Journal Respir Res Section Body Doc Link PMC548519 Disease Relevance 0.32 Pain Relevance 0.11
LM8 cells express mainly MMP-2 [16].
Gene_expression (express) of MMP-2
11) Confidence 0.59 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 1.33 Pain Relevance 0
Assay of MMP-2 by gelatin zymography
Gene_expression (Assay) of MMP-2
12) Confidence 0.59 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 0 Pain Relevance 0
The results of immunohistochemistry (Figure 6A) and gelatin zymography (Figure 6B) showed that the tumors of the TGZ group exhibited lower expression and activity of MMP-2 compared with the control group.
Gene_expression (expression) of MMP-2 associated with cancer
13) Confidence 0.59 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2838820 Disease Relevance 1.26 Pain Relevance 0
Because recent evidence suggests that MT1-MMP (but not MMP-2 or MMP-9) express proteolytic activity that mediates fibroblast migration through type I collagen [14] and MMP-2 and MMP-9 deficient mice develop normally, it is possible that MMP-2 or MMP-9 play a role in more complex models of tumor invasion or growth because they disrupt tumor-stromal signaling rather than matrix degradation.
Neg (not) Gene_expression (express) of MMP-2 in fibroblast associated with cancer and metalloproteinase
14) Confidence 0.58 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1450297 Disease Relevance 0.87 Pain Relevance 0.98
MMP-2 null serum was used for MMP-2 null experiments since MMP-2 is produced in the serum.
Gene_expression (produced) of MMP-2 associated with metalloproteinase
15) Confidence 0.58 Published 2006 Journal BMC Cancer Section Body Doc Link PMC1450297 Disease Relevance 0.23 Pain Relevance 0.53
Interestingly, MMP2 expression was only very low (not shown).
Gene_expression (expression) of MMP2
16) Confidence 0.57 Published 2010 Journal J Cardiothorac Surg Section Body Doc Link PMC2933604 Disease Relevance 0.44 Pain Relevance 0.19
Lung metastases, MMP2 activity, protein levels of MMP2, TIMP2, and VEGF, and microvessel density (MVD) were determined.


Gene_expression (levels) of MMP2 in Lung associated with metastasis
17) Confidence 0.56 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.91 Pain Relevance 0.17
The in situ activities of membrane type 1-matrix metalloproteinase (MT1-MMP), matrix metalloproteinase 2 (MMP2), and protein levels of MMP2, tissue inhibitor of metalloproteinase 2 (TIMP2), vascular endothelial growth factor (VEGF), and endostatin in the grown tumors obtained from the implantation sites were determined.
Gene_expression (levels) of MMP2 associated with cancer and metalloproteinase
18) Confidence 0.56 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.62 Pain Relevance 0.29
Protein levels of MMP2, TIMP2, VEGF, and endostatin in tumor extracts were measured via commercial available MMP2 (R&D Systems, Minneapolis, MN), TIMP2 (Amersham Biosciences, Buckinghamshire, UK), VEGF enzyme-linked immunosorbent assay (ELISA; R&D Systems, Minneapolis, MN), and endostatin (Chemicon International, Temecula, CA) kits.
Gene_expression (levels) of MMP2 associated with cancer
19) Confidence 0.56 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.17 Pain Relevance 0
The in situ activities of membrane type 1-matrix metalloproteinase (MT1-MMP), matrix metalloproteinase 2 (MMP2), and protein levels of MMP2, tissue inhibitor of metalloproteinase 2 (TIMP2), vascular endothelial growth factor (VEGF), and endostatin in the grown tumors obtained from the implantation sites were determined.
Gene_expression (levels) of MMP2 associated with cancer and metalloproteinase
20) Confidence 0.56 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2976755 Disease Relevance 0.62 Pain Relevance 0.29

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