INT95607

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.60
First Reported 2001
Last Reported 2010
Negated 3
Speculated 0
Reported most in Body
Documents 19
Total Number 19
Disease Relevance 7.86
Pain Relevance 6.18

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 (MMP1) extracellular region (MMP1) proteinaceous extracellular matrix (MMP1)
Anatomy Link Frequency
blood 2
outflow 1
joint 1
bladder 1
MMP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 668 100.00 Very High Very High Very High
Osteoarthritis 172 100.00 Very High Very High Very High
Inflammation 74 100.00 Very High Very High Very High
Adalimumab 4 99.10 Very High Very High Very High
rheumatoid arthritis 11 98.56 Very High Very High Very High
methotrexate 2 87.84 High High
antagonist 7 82.72 Quite High
Pain 7 74.84 Quite High
Analgesic 4 73.16 Quite High
cytokine 65 70.16 Quite High
Disease Link Frequency Relevance Heat
Osteoarthritis 176 100.00 Very High Very High Very High
INFLAMMATION 82 100.00 Very High Very High Very High
Transitional Cell Carcinoma 130 99.04 Very High Very High Very High
Rheumatoid Arthritis 14 98.56 Very High Very High Very High
Cancer 211 98.44 Very High Very High Very High
Disease 51 94.28 High High
Bladder Cancer 145 90.72 High High
Malignant Neoplastic Disease 16 90.68 High High
Metastasis 61 89.56 High High
Necrosis 9 85.56 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Regulation of MMPs is aberrant in osteoarthritis and RA, and MMPs have been implicated in the collagen breakdown that contributes to joint destruction in these diseases.
Regulation (Regulation) of MMP in joint associated with rheumatoid arthritis, metalloproteinase, disease and osteoarthritis
1) Confidence 0.60 Published 2001 Journal Drugs Aging Section Abstract Doc Link 11346130 Disease Relevance 1.21 Pain Relevance 0.87
Activated MMP1, MMP3 and latent forms of MMP2 and MMP9 are regulated and inhibited by endogenous proteins known as tissue inhibitors of metalloproteinase TIMP1 and TIMP2 [17].
Regulation (regulated) of MMP1 associated with metalloproteinase
2) Confidence 0.50 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.88 Pain Relevance 0.23
Comparing our data on different MMPs MMP2 was proved to be the best marker alone.
Regulation (different) of MMP associated with metalloproteinase
3) Confidence 0.44 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.61 Pain Relevance 0.18
g) was used as a positive control for caseinolytic activities and bacterial collagenase (10 ?
Regulation (control) of collagenase
4) Confidence 0.29 Published 2004 Journal BMC Musculoskelet Disord Section Body Doc Link PMC404466 Disease Relevance 0 Pain Relevance 0.08
PGAs appear to regulate matrix metalloproteinases (MMP) and tissue inhibitors of matrix metalloproteinases (TIMP) to modulate trabecular outflow resistance.
Regulation (regulate) of MMP in outflow associated with metalloproteinase
5) Confidence 0.26 Published 2010 Journal Clinical Ophthalmology (Auckland, N.Z.) Section Body Doc Link PMC2915861 Disease Relevance 0.21 Pain Relevance 0.40
In this study the concentrations of MMP1, MMP2, MMP3, MMP9, their inhibitors TIMP1, TIMP2, and the MMP1/TIMP1-complex (MTC1) were quantified in blood plasma with the sandwich enzyme-linked immunosorbent assay (ELISA).
Regulation (concentrations) of MMP1 in blood
6) Confidence 0.22 Published 2006 Journal BMC Urol Section Abstract Doc Link PMC1560390 Disease Relevance 0.44 Pain Relevance 0.13
The plasma concentration of MMP2 was significantly higher in comparison to the control group whereas the concentrations of MMP1, TIMP1, TIMP2, and MTC1 were significantly lower from patients with non-metastasized TCC of the bladder in comparison to the healthy control group (Table I).
Regulation (concentrations) of MMP1 in bladder associated with transitional cell carcinoma
7) Confidence 0.22 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.64 Pain Relevance 0.19
In this study the concentrations of MMP1, MMP2, MMP3, MMP9, their inhibitors TIMP1, TIMP2, and the MMP1/TIMP1-complex (MTC1) were quantified in blood plasma with the sandwich enzyme-linked immunosorbent assay (ELISA).
Regulation (concentrations) of MMP1 in blood
8) Confidence 0.22 Published 2006 Journal BMC Urol Section Abstract Doc Link PMC1560390 Disease Relevance 0.44 Pain Relevance 0.13
There were no significant differences in MMP-1 and MMP-3 concentrations between the groups (data not shown).


Neg (no) Regulation (differences) of MMP-1 associated with metalloproteinase
9) Confidence 0.20 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0.06 Pain Relevance 0.85
With regard to structural mediators, diacerein decreased MMP-13 levels in synoviocytes but did not modify MMP-1 presence.
Neg (not) Regulation (modify) of MMP-1
10) Confidence 0.17 Published 2008 Journal Rheumatology (Oxford) Section Body Doc Link 18375401 Disease Relevance 0.06 Pain Relevance 0
LPS-induced IL-6 and PGE2 release was only slightly inhibited at high doses, whereas LPS-induced release of IL-8 and matrix metalloprotease (MMP)-9 was not affected.
Regulation (affected) of matrix metalloprotease
11) Confidence 0.15 Published 2004 Journal Scand. J. Rheumatol. Suppl. Section Abstract Doc Link 15515409 Disease Relevance 0.49 Pain Relevance 0.19
In adalimumab recipient, radiographic progression is also controlled and serum levels of matrix metalloproteinase-1(MMP-1) and MMP-3 decrease.
Regulation (controlled) of MMP-1 associated with metalloproteinase and adalimumab
12) Confidence 0.15 Published 2002 Journal Nippon Rinsho Section Abstract Doc Link 12510366 Disease Relevance 0.40 Pain Relevance 0.34
The concentrations of MMP-1 and MMP-3 were generally low in all the samples.
Regulation (concentrations) of MMP-1 associated with metalloproteinase
13) Confidence 0.12 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0.07 Pain Relevance 0.80
Researchers have identified that the long-chain fatty acids could inhibit MMPs. however for different MMPs the degree of inhibition is different, such as oleic acid, elaidic acid can inhibit MMP-2 and MMP-9 with the micromol Ki values, although their inhibitory effects on collagenase-1 (MMP-1) are weak, as assessed using synthetic or natural substrates [42].
Regulation (effects) of MMP-1 associated with metalloproteinase
14) Confidence 0.11 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.22 Pain Relevance 0.17
Researchers have identified that the long-chain fatty acids could inhibit MMPs. however for different MMPs the degree of inhibition is different, such as oleic acid, elaidic acid can inhibit MMP-2 and MMP-9 with the micromol Ki values, although their inhibitory effects on collagenase-1 (MMP-1) are weak, as assessed using synthetic or natural substrates [42].
Regulation (effects) of collagenase-1 associated with metalloproteinase
15) Confidence 0.11 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.22 Pain Relevance 0.17
This suggests that these inhibitors are specific for the ET-1-activated pathways since they do not affect the basal levels of MMP-1 and MMP-13.
Neg (not) Regulation (affect) of MMP-1
16) Confidence 0.10 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1065327 Disease Relevance 0.22 Pain Relevance 0.15
To determine the functional consequence of PAR-2 activation, we studied some of the major catabolic/inflammatory factors involved in OA pathophysiology, including MMP-1, MMP-13, and COX-2 (Figure 4).
Regulation (some) of MMP-1 associated with inflammation, metalloproteinase and osteoarthritis
17) Confidence 0.09 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2246240 Disease Relevance 0.77 Pain Relevance 0.66
To determine the functional consequence of PAR-2 activation, we studied some of the major catabolic/inflammatory factors involved in OA pathophysiology, including MMP-1, MMP-13, and COX-2 (Figure 4).
Regulation (involved) of MMP-1 associated with inflammation, metalloproteinase and osteoarthritis
18) Confidence 0.09 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2246240 Disease Relevance 0.71 Pain Relevance 0.62
Such a dose response is consistent with other studies which have demonstrated, not only a similar effect on MMP-1 and MMP-3 at the protein and mRNA level [39-43], but also that a threshold of serum concentration of CSA helps to govern this mechanism [44-49].
Regulation (effect) of MMP-1
19) Confidence 0.04 Published 2010 Journal J Inflamm (Lond) Section Body Doc Link PMC2949711 Disease Relevance 0.20 Pain Relevance 0.05

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox