INT82871

From wiki-pain
Revision as of 01:13, 24 September 2012 by Daniel (Talk | contribs)

(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to: navigation, search
Context Info
Confidence 0.96
First Reported 1999
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 13
Total Number 13
Disease Relevance 10.71
Pain Relevance 4.09

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
extracellular matrix 5
plaque 2
joint 1
endothelial cells 1
MMP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 157 100.00 Very High Very High Very High
Inflammation 80 96.28 Very High Very High Very High
Angina 13 95.88 Very High Very High Very High
Chronic pancreatitis 99 90.16 High High
Sicca syndrome 33 85.96 High High
cytokine 75 82.32 Quite High
rheumatoid arthritis 18 82.32 Quite High
fibrosis 25 75.00 Quite High
Demyelination 3 75.00 Quite High
Peripheral nervous system 1 70.88 Quite High
Disease Link Frequency Relevance Heat
Atherosclerotic Plaque 4 99.08 Very High Very High Very High
Cancer 52 98.48 Very High Very High Very High
Rupture 12 98.44 Very High Very High Very High
Primary Sclerosing Cholangitis 231 97.68 Very High Very High Very High
Sprains And Strains 22 97.36 Very High Very High Very High
Increased Venous Pressure Under Development 3 96.56 Very High Very High Very High
INFLAMMATION 87 96.28 Very High Very High Very High
Cv General 3 Under Development 12 95.88 Very High Very High Very High
Myocardial Infarction 8 95.20 Very High Very High Very High
Metastasis 11 94.20 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Matrix metalloproteinases (MMPs) degrade all protein components of the extracellular matrix.
Protein_catabolism (degrade) of MMP in extracellular matrix associated with metalloproteinase
1) Confidence 0.96 Published 1999 Journal Neurology Section Abstract Doc Link 10408531 Disease Relevance 0.71 Pain Relevance 0.43
Furthermore, matrix degradation by MMPs may cause the plaque instability and rupture that leads to the clinical symptoms of atherosclerosis; unstable angina, myocardial infarction and stroke.
Protein_catabolism (degradation) of MMP in plaque associated with angina, stroke, rupture, metalloproteinase, increased venous pressure under development and myocardial infarction
2) Confidence 0.96 Published 2000 Journal Expert Opin Investig Drugs Section Abstract Doc Link 11060722 Disease Relevance 0.82 Pain Relevance 0.40
Matrix metalloproteinases (MMPs) play an important role in cardiovascular remodeling by degrading the extracellular matrix.
Protein_catabolism (degrading) of MMP in extracellular matrix associated with metalloproteinase
3) Confidence 0.96 Published 2003 Journal Clin Cardiol Section Abstract Doc Link 12625594 Disease Relevance 0.33 Pain Relevance 0.26
Matrix metalloproteinases (MMPs) are important for resorption of extracellular matrixes and may degrade the fibrous cap of an atherosclerotic plaque, thus contributing to coronary plaque rupture.
Protein_catabolism (degrade) of MMP in plaque associated with atherosclerotic plaque, rupture and metalloproteinase
4) Confidence 0.96 Published 2006 Journal Am. J. Cardiol. Section Abstract Doc Link 16442358 Disease Relevance 1.02 Pain Relevance 0.55
The principal function of MMPs is the proteolytic degradation of connective tissue matrix proteins, and in concert they can degrade practically all extracellular matrix proteins [5].
Protein_catabolism (degradation) of MMP in extracellular matrix associated with metalloproteinase
5) Confidence 0.86 Published 2007 Journal J Negat Results Biomed Section Body Doc Link PMC2235889 Disease Relevance 2.18 Pain Relevance 0.61
Matrix metalloproteinases (MMPs) belong to the group of ECM degradation enzymes.
Protein_catabolism (degradation) of MMP in ECM associated with metalloproteinase
6) Confidence 0.86 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 1.12 Pain Relevance 0.31
These studies have shown that high strains (or long duty cycles) applied by stretching bioreactors can cause tenocytes to produce abnormal levels of matrix metalloproteases (MMPs), which would in turn degrade the collagen and cause degeneration [131,137-144].
Protein_catabolism (degrade) of MMP associated with sprains and strains
7) Confidence 0.86 Published 2009 Journal Sports Med Arthrosc Rehabil Ther Technol Section Body Doc Link PMC2695438 Disease Relevance 0.91 Pain Relevance 0.03
Matrix metalloproteinases (MMPs) are a family of zinc-containing enzymes involved in the degradation and remodeling of extracellular matrix proteins.
Protein_catabolism (degradation) of MMP in extracellular matrix associated with metalloproteinase
8) Confidence 0.86 Published 2004 Journal Curr. Med. Chem. Section Abstract Doc Link 15544483 Disease Relevance 0.28 Pain Relevance 0.29
While earlier it was thought that collagenolytic activity could be attributed to collagenases and caseinolytic activities to stromelysin, it was shown meanwhile that mainly collagen can be degraded by several neutral metalloproteinases (MMP1,8,13, MT-1)[47,48].
Protein_catabolism (degraded) of MMP1 associated with metalloproteinase
9) Confidence 0.65 Published 2004 Journal BMC Musculoskelet Disord Section Body Doc Link PMC404466 Disease Relevance 0.30 Pain Relevance 0.22
Furthermore, the matrix degradation enzyme MMP-1 was induced (LPS by 46%; TNFalpha by 454%), while its inhibitor TIMP-2 was suppressed (by 20% and 18%, respectively; data not shown).
Protein_catabolism (degradation) of MMP-1
10) Confidence 0.15 Published 2007 Journal J Transl Med Section Body Doc Link PMC2234395 Disease Relevance 0.55 Pain Relevance 0.04
Moreover, this site specific variance in ECM deposition can be due to the following reasons: 1) The packed immune clusters are actually forming in expanded perivascular spaces as hinted by the presence of central CD31 positive endothelial cells; 2) In vitro, the matrix degradation enzyme MMP-1 was increased together with an increase in ECM proteins collagen1 and fibronectin; 3) High amounts of TNFalpha exert cytotoxic effects on PSC [20] which is probably represented in vivo as a function of their density.
Protein_catabolism (degradation) of MMP-1 in endothelial cells associated with primary sclerosing cholangitis
11) Confidence 0.15 Published 2007 Journal J Transl Med Section Body Doc Link PMC2234395 Disease Relevance 0.60 Pain Relevance 0.03
Fibrillar collagen is resistant to proteolytic degradation but at neutral pH is susceptible to degradation from the collagenases MMP-1, MMP-8 and MMP-13 that are all found within the joint.
Protein_catabolism (degradation) of MMP-1 in joint
12) Confidence 0.14 Published 2003 Journal Arthritis Res Ther Section Body Doc Link PMC154424 Disease Relevance 0.25 Pain Relevance 0.04
LPS and TNFalpha induced collagen1 and fibronectin levels as well as the matrix degradation enzyme MMP-1.
Protein_catabolism (degradation) of MMP-1
13) Confidence 0.10 Published 2007 Journal J Transl Med Section Abstract Doc Link PMC2234395 Disease Relevance 1.62 Pain Relevance 0.88

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox