INT173587

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Context Info
Confidence 0.32
First Reported 2003
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 59
Total Number 62
Disease Relevance 32.73
Pain Relevance 8.96

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular region (COL5A2) molecular_function (COL5A2)
Anatomy Link Frequency
cartilage 7
joint 5
cleavage 4
plaque 4
osteoclasts 2
COL5A2 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 1393 99.92 Very High Very High Very High
Osteoarthritis 1296 99.84 Very High Very High Very High
cytokine 234 98.74 Very High Very High Very High
chemokine 15 92.32 High High
Inflammation 384 92.00 High High
Arthritis 314 90.60 High High
withdrawal 14 86.88 High High
lidocaine 11 82.44 Quite High
Angina 38 82.32 Quite High
rheumatoid arthritis 225 81.08 Quite High
Disease Link Frequency Relevance Heat
Penile Induration 55 100.00 Very High Very High Very High
Breast Cancer 774 99.86 Very High Very High Very High
Osteoarthritis 410 99.84 Very High Very High Very High
Targeted Disruption 62 99.64 Very High Very High Very High
Cancer 607 99.24 Very High Very High Very High
Atherosclerotic Plaque 10 99.16 Very High Very High Very High
Rupture 127 99.12 Very High Very High Very High
Arthropathy 68 98.96 Very High Very High Very High
Skin Cancer 25 98.56 Very High Very High Very High
Acute Coronary Syndrome 72 98.44 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These studies provide a rationale for the use of this ELISA to follow type II collagen degradation in response to therapy.


Protein_catabolism (degradation) of collagen
1) Confidence 0.32 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.86 Pain Relevance 0.19
This proteolysis causes a loss of type II collagen epitopes to body fluids wherein they can indicate the amount of degradation of collagen.
Protein_catabolism (degradation) of collagen in body
2) Confidence 0.32 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.06 Pain Relevance 0.08
Type II collagen is possibly the ideal marker of cartilage degradation.
Protein_catabolism (degradation) of collagen in cartilage
3) Confidence 0.28 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0 Pain Relevance 0.04
After the initial cleavage of the collagen triple helix by collagenase, the helix can denature into the monomeric ?
Protein_catabolism (cleavage) of collagen in cleavage
4) Confidence 0.21 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.82 Pain Relevance 0.18
What threshold level of collagen degradation or synthesis in a particular joint is required to impact serum or urine concentrations?
Protein_catabolism (degradation) of collagen in joint
5) Confidence 0.21 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.60 Pain Relevance 0.25
The process of collagen cleavage and denaturation of the triple helical molecule exposes certain protein sequences, termed neoepitopes, within the collagen molecule.
Protein_catabolism (cleavage) of collagen in cleavage
6) Confidence 0.21 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.08 Pain Relevance 0.04
Simultaneous assessment of both collagen degradation and synthesis in a patient is a particularly promising approach for diagnosing and determining risk of OA progression (Poole, 2003).
Protein_catabolism (degradation) of collagen associated with osteoarthritis
7) Confidence 0.21 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.51 Pain Relevance 0.26
Matrix turnover (degradation of damaged collagen by MMPs, and its replacement by newly synthesised collagen) in turn is a function of the cells present in the tendon.
Protein_catabolism (degradation) of collagen in tendon
8) Confidence 0.19 Published 2008 Journal J Orthop Surg Section Body Doc Link PMC2515295 Disease Relevance 0.10 Pain Relevance 0
The urinary Type II Collagen NeoEpitope (uTIINE) is detected by a sandwich ELISA with specificity for type II collagen degradation.
Protein_catabolism (degradation) of collagen
9) Confidence 0.18 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.59 Pain Relevance 0.30
The ability to monitor and slow or reverse this process has important clinical and therapeutic implications because extensive degradation of mature cross-linked type II collagen fibers is considered to be a critical and perhaps irreversible stage in joint destruction (Billinghurst et al. 1997; Nelson et al. 1998).


Protein_catabolism (degradation) of collagen in joint
10) Confidence 0.18 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.06 Pain Relevance 0.07
Amino-terminal telopeptides of type II collagen (Col2NTx) have not been found in body fluids, suggesting they are degraded in vivo all the way to free hydroxylysylpyridinoline.
Protein_catabolism (degraded) of collagen in body
11) Confidence 0.18 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.66 Pain Relevance 0.20
Type II collagen is cleaved by collagenases known as metalloproteinases (MMPs); MMP-1, 8, and 13 are thought to be particularly important.
Protein_catabolism (cleaved) of collagen associated with metalloproteinase
12) Confidence 0.18 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.08 Pain Relevance 0.09
After grafting, a biodegradable collagen membrane of porcine origin (Bio-Gide®, Geistlich AG, Wolhusen, Switzerland) was trimmed and adapted over the NBM using a double-layer technique to retard the resorption of the barrier [3] (Fig. 5).
Protein_catabolism (biodegradable) of collagen
13) Confidence 0.15 Published 2008 Journal Clin Oral Investig Section Body Doc Link PMC2491434 Disease Relevance 0 Pain Relevance 0
The data presented in this paper clearly demonstrate that human breast carcinoma cell lines have the capacity to degrade the organic aspect of bone matrix in vitro, and there is a dependency on the PA system for the cell-mediated collagen degradation.
Protein_catabolism (degradation) of collagen associated with breast cancer
14) Confidence 0.09 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.37 Pain Relevance 0.04
Interestingly, the depletion of plasminogen from serum also completely blocked breast cancer cell mediated collagen dissolution, implicating the PAS in breast cancer-mediated collagen degradation (Fig. 1).
Protein_catabolism (degradation) of collagen associated with breast cancer
15) Confidence 0.09 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.67 Pain Relevance 0.03
In accordance with this finding, the breast cancer cells degraded collagen under serum-free conditions only when supplemented by exogenous plasminogen (Fig. 1).
Protein_catabolism (degraded) of collagen associated with breast cancer
16) Confidence 0.09 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.66 Pain Relevance 0
At the end of the culture period the media were centrifuged (15 min, 1200 × g) to remove any collagen fibrils, and radioactivity released during collagen degradation quantified by liquid scintillation counting.
Protein_catabolism (degradation) of collagen
17) Confidence 0.09 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.07 Pain Relevance 0
During cartilage degeneration (that is, in osteoarthritis (OA)), the collagen matrix degrades and the GAG concentration diminishes, resulting in a severity-dependent decreased tonicity of between 280 and 350 mOsm [3,6].
Protein_catabolism (degrades) of collagen in cartilage associated with osteoarthritis
18) Confidence 0.08 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2911888 Disease Relevance 0.25 Pain Relevance 0.10
We have therefore assessed the ability of three human breast cancer cell lines, MDA-MB-231 (MDA-231), ZR-75-1 and MCF-7 to degrade bone collagen in vitro using matrix degradation assays and compared their effects with those of a normal breast epithelial cell line, HME.
Protein_catabolism (degrade) of collagen in MCF-7 associated with breast cancer
19) Confidence 0.06 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.93 Pain Relevance 0.16
When aprotinin, which inhibits both plasmin bound to the cell surface and plasmin in solution, was added, collagen degradation was also completely blocked (Fig. 6).
Protein_catabolism (degradation) of collagen
20) Confidence 0.06 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.53 Pain Relevance 0.11

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