INT107606

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Context Info
Confidence 0.42
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 38
Total Number 39
Disease Relevance 11.94
Pain Relevance 10.01

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
fibroblasts 2
macrophage 1
chondrocytes 1
osteoclast 1
periodontal ligament 1
MMP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 1008 100.00 Very High Very High Very High
Osteoarthritis 230 99.44 Very High Very High Very High
cytokine 232 99.28 Very High Very High Very High
Adalimumab 133 97.94 Very High Very High Very High
Arthritis 237 96.92 Very High Very High Very High
sodium channel 20 96.40 Very High Very High Very High
Inflammatory stimuli 11 95.24 Very High Very High Very High
rheumatoid arthritis 262 94.04 High High
Inflammatory response 8 89.00 High High
Calcium channel 4 88.72 High High
Disease Link Frequency Relevance Heat
Osteoarthritis 249 99.44 Very High Very High Very High
Chondrosarcoma 66 99.28 Very High Very High Very High
Hypertrophy 22 98.84 Very High Very High Very High
Rheumatoid Arthritis 266 98.40 Very High Very High Very High
Arthritis 314 96.92 Very High Very High Very High
Gingival Overgrowth 40 96.20 Very High Very High Very High
INFLAMMATION 302 94.92 High High
Cancer 193 94.88 High High
Osteoporosis 29 92.48 High High
Aging 3 91.60 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This may be attributed in part to the downregulation of serum matrix metalloproteinase (MMP)-1 and MMP-3 following anti-TNF therapy, as well as downregulating the role of TNF in osteoclast maturation and activation (Brennan et al 1997; Catrina et al 2002, 2006).


Negative_regulation (downregulation) of MMP in osteoclast associated with metalloproteinase
1) Confidence 0.42 Published 2007 Journal Therapeutics and Clinical Risk Management Section Body Doc Link PMC1936294 Disease Relevance 0.89 Pain Relevance 0.89
The increased protein levels of MMP-1 and MMP-3 were also reduced by 1000 microg/ml HA.
Negative_regulation (reduced) of MMP-1 associated with metalloproteinase
2) Confidence 0.37 Published 2004 Journal Tohoku J. Exp. Med. Section Abstract Doc Link 15383690 Disease Relevance 0.20 Pain Relevance 0.89
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].
Negative_regulation (inhibited) of MMP1 associated with metalloproteinase
3) Confidence 0.35 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.89 Pain Relevance 0.23
and LG268 leads to modest but significant inhibition of MMP-1 and MMP-13, and a 12- to 24-hour pretreatment is necessary for maximum inhibition of MMP levels in these cells by the RXR ligand, LG268 [21].
Negative_regulation (inhibition) of MMP-1
4) Confidence 0.34 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.23 Pain Relevance 0.12
As shown in Figure 3a, treatment with either LG268 or rosiglitazone effectively reduced MMP-1 and MMP-13 mRNA by approximately 50%, and treatment with both ligands led to significantly greater inhibition (approximately 75%) than either drug alone.
Negative_regulation (reduced) of MMP-1
5) Confidence 0.34 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0 Pain Relevance 0
With rosiglitazone, both the maximum level of inhibition of MMP-1 and MMP-13 (50% to 60%) and the pattern of MMP inhibition mirror those previously seen with LG268 treatment [21], suggesting that these compounds may be acting through similar mechanisms.


Negative_regulation (inhibition) of MMP-1
6) Confidence 0.34 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.05 Pain Relevance 0.10
Real-time RT-PCR was used to quantify MMP mRNA, and Figure 1 demonstrates a dose-dependent inhibition of MMP-1 and MMP-13 mRNA levels in response to rosiglitazone treatment.
Negative_regulation (inhibition) of MMP-1
7) Confidence 0.34 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.21 Pain Relevance 0.17
to a degenerate DR-1 site as central to the inhibition of rabbit MMP-1 by rosiglitazone, and initial evidence suggested that the inhibition was due to competition between PPAR?
Negative_regulation (inhibition) of MMP-1
8) Confidence 0.34 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.07 Pain Relevance 0
In adalimumab recipient, radiographic progression is also controlled and serum levels of matrix metalloproteinase-1(MMP-1) and MMP-3 decrease.
Negative_regulation (decrease) of MMP-1 associated with metalloproteinase and adalimumab
9) Confidence 0.32 Published 2002 Journal Nippon Rinsho Section Abstract Doc Link 12510366 Disease Relevance 0.39 Pain Relevance 0.34
and AP-1 proteins as a possible mechanism for rosiglitazone-mediated inhibition of MMP-1 [17].
Negative_regulation (inhibition) of MMP-1
10) Confidence 0.30 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.08 Pain Relevance 0.04
Because of the conserved nature of NHR domain structures, K364 may be the required RXR SUMOylation site for inhibition of MMP-1 and MMP-13 through this mechanism.


Negative_regulation (inhibition) of MMP-1
11) Confidence 0.25 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.24 Pain Relevance 0
Figure 3 shows a decrease in expression of MMP-1 and MMP-13 at the transcriptional level in cells treated with LG268 and rosiglitazone.
Negative_regulation (decrease) of MMP-1
12) Confidence 0.25 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0 Pain Relevance 0
-induced MMP-1 and MMP-13 transcription in the SW-1353 human chondrosarcoma cell line and is associated with a decrease in histone acetylation proximal to the transcription start site in the MMP-1 and MMP-13 promoters [21].
Negative_regulation (decrease) of MMP-1 in proximal associated with chondrosarcoma
13) Confidence 0.25 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.21 Pain Relevance 0.06
, and RXR homodimers bind to the DR-1 element [11], suggesting that all or any of these three dimers may be responsible for mediating the inhibitory effect of LG268 on MMP-1 and MMP-13.
Negative_regulation (effect) of MMP-1
14) Confidence 0.25 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0.15 Pain Relevance 0.04
, which appeared to be blocked by ligand treatment at the MMP-1 promoter but only modestly inhibited at the MMP-13 promoter (Figure 6).
Negative_regulation (blocked) of MMP-1
15) Confidence 0.25 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2656243 Disease Relevance 0 Pain Relevance 0
In fibroblasts, osteopontin up-regulated tissue inhibitor of metalloprotease-1 and type I collagen, and down-regulated matrix metalloprotease-1 (MMP-1) expression, while in A549 cells it caused up-regulation of MMP-7.
Negative_regulation (inhibitor) of metalloprotease-1 in A549
16) Confidence 0.23 Published 2005 Journal PLoS Medicine Section Abstract Doc Link PMC1198037 Disease Relevance 0.66 Pain Relevance 0.31
The inhibitory effect of osteopontin on MMP-1 was also observed at the protein level by Western blot analysis.
Negative_regulation (effect) of MMP-1
17) Confidence 0.22 Published 2005 Journal PLoS Medicine Section Body Doc Link PMC1198037 Disease Relevance 0 Pain Relevance 0
Additionally, we observed a concomitant increase in TIMP-1, the main inhibitor of MMP-1 (as well as MMP-2 and ?
Negative_regulation (inhibitor) of MMP-1
18) Confidence 0.22 Published 2005 Journal PLoS Medicine Section Body Doc Link PMC1198037 Disease Relevance 0.42 Pain Relevance 0.17
As shown in Figure 6D, the level of immunoreactive MMP-1 present in the conditioned medium was decreased in the fibroblasts stimulated with osteopontin as compared with control cells.


Negative_regulation (decreased) of MMP-1 in fibroblasts
19) Confidence 0.20 Published 2005 Journal PLoS Medicine Section Body Doc Link PMC1198037 Disease Relevance 0 Pain Relevance 0
The results revealed that NeovastatÃ’ inhibits enzymatic activity of MMP-2 with minor inhibition of MMP-1, -7, -9 and -13.
Negative_regulation (inhibition) of MMP-1
20) Confidence 0.14 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.08 Pain Relevance 0.12

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