INT173511

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Context Info
Confidence 0.21
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 4
Disease Relevance 2.73
Pain Relevance 2.39

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 (Mmp1a) extracellular region (Mmp1a) proteinaceous extracellular matrix (Mmp1a)
Anatomy Link Frequency
cartilage 1
smooth muscle cells 1
fibroblasts 1
Mmp1a (Mus musculus)
Pain Link Frequency Relevance Heat
metalloproteinase 90 100.00 Very High Very High Very High
rheumatoid arthritis 116 99.90 Very High Very High Very High
fibrosis 47 97.28 Very High Very High Very High
Inflammation 84 92.40 High High
cytokine 44 87.68 High High
Inflammatory response 6 83.52 Quite High
Pain 2 77.36 Quite High
Arthritis 68 62.40 Quite High
Multiple sclerosis 25 58.88 Quite High
Angina 10 47.84 Quite Low
Disease Link Frequency Relevance Heat
Rheumatoid Arthritis 116 99.90 Very High Very High Very High
Pulmonary Fibrosis 28 97.28 Very High Very High Very High
INFLAMMATION 78 92.40 High High
Pulmonary Disease 3 87.52 High High
Acute Coronary Syndrome 17 81.56 Quite High
Pain 1 77.36 Quite High
Colitis 1 77.04 Quite High
Coronary Artery Disease 6 65.20 Quite High
Adhesions 13 63.28 Quite High
Arthritis 75 62.40 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
PDE4 inhibitor cilomilast was also shown to suppress the release and activation of MMP-1 and MMP-9 from lung fibroblasts, which are known to be involved in PF progression [18].
Localization (release) of MMP-1 in fibroblasts associated with fibrosis
1) Confidence 0.21 Published 2010 Journal BMC Pulm Med Section Body Doc Link PMC2881047 Disease Relevance 0.71 Pain Relevance 0.24
not only increased the synthetic secretion of MMP-1, but also activated MMP-2 and MMP-9 in the form of zymogen and started to synthesize and secrete MMP-3.1,5 Although the activity of MMPs is inhibited by its tissue inhibitors of metalloproteinase (TIMP), normally vascular smooth muscle cells will secrete a tiny amount of TIMP-1 and TIMP-2 for modulation and cytokine which does nothing to its secretion.
Localization (secretion) of MMP-1 in smooth muscle cells associated with metalloproteinase and cytokine
2) Confidence 0.18 Published 2010 Journal Clinical Medicine Insights. Cardiology Section Body Doc Link PMC2956475 Disease Relevance 0.74 Pain Relevance 0.75
, IL-6, MMP-1 and TIMP was observed in synovial tissue from RA patients after IFN-?
Localization (observed) of MMP-1 associated with rheumatoid arthritis
3) Confidence 0.13 Published 2002 Journal Arthritis Res Section Body Doc Link PMC153843 Disease Relevance 0.54 Pain Relevance 0.31
Of note, however, RA FLS secreted >100 fold more MMP-1 than MMP-13 under the same in vitro conditions, implying that perhaps production of MMP-1 by FLS is more important than that of MMP-13 in catalysing cartilage degradation in RA.
Localization (secreted) of MMP-1 in cartilage associated with metalloproteinase and rheumatoid arthritis
4) Confidence 0.10 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2888198 Disease Relevance 0.74 Pain Relevance 1.09

General Comments

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