INT103244

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Context Info
Confidence 0.72
First Reported 2002
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 12
Total Number 12
Disease Relevance 11.81
Pain Relevance 2.01

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 (MMP9) extracellular space (MMP9) extracellular region (MMP9)
proteinaceous extracellular matrix (MMP9) extracellular matrix organization (MMP9) protein complex (MMP9)
Anatomy Link Frequency
Neutrophil 2
osteoclasts 1
extracellular matrix 1
lung 1
MMP9 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 73 100.00 Very High Very High Very High
Inflammatory response 15 99.28 Very High Very High Very High
Inflammation 142 98.68 Very High Very High Very High
aspirin 10 94.32 High High
cytokine 19 94.28 High High
alcohol 36 89.24 High High
Nicotine 192 86.20 High High
cINOD 4 79.64 Quite High
Inflammatory mediators 6 76.16 Quite High
chemokine 5 52.96 Quite High
Disease Link Frequency Relevance Heat
Metastasis 66 100.00 Very High Very High Very High
Cancer 187 99.50 Very High Very High Very High
INFLAMMATION 169 99.28 Very High Very High Very High
Osteolysis 8 97.72 Very High Very High Very High
Necrosis 4 96.24 Very High Very High Very High
Chronic Obstructive Pulmonary Disease 54 96.12 Very High Very High Very High
Disease 148 95.44 Very High Very High Very High
Skin Cancer 2 95.32 Very High Very High Very High
Increased Venous Pressure Under Development 38 93.20 High High
Bone Cancer 2 92.88 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Each group was compared with normal lung tissue with respect to tissue collagen and collagen degradation product content (hydroxyproline assay), gelatinolytic activity (zymography) and the expression of matrix metalloproteinases, MMP-2 and MMP-9 (Western immunoblot).
Protein_catabolism (degradation) of MMP-9 in lung associated with metalloproteinase
1) Confidence 0.72 Published 2002 Journal Eur. J. Pharmacol. Section Abstract Doc Link 12044784 Disease Relevance 0.65 Pain Relevance 0.38
This could possibly be due to a relatively short period of time passing between sample date and analysis, as MMP-9 has been shown to degrade even at low temperature [31].
Protein_catabolism (degrade) of MMP-9
2) Confidence 0.65 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2258002 Disease Relevance 0.35 Pain Relevance 0.14
The matrix degrading enzyme MMP-9 is highly expressed at sites of inflammation and contributes to the pathogenesis of various chronic inflammatory diseases.
Protein_catabolism (degrading) of MMP-9 associated with inflammation and disease
3) Confidence 0.64 Published 2006 Journal J Inflamm (Lond) Section Body Doc Link PMC1413525 Disease Relevance 0.86 Pain Relevance 0.31
Fibrinogen is degraded by MMP9 [39–41], and the fibrinogen degradation fragments have been shown to be biologically important molecules with numerous pro-inflammatory actions [42].
Protein_catabolism (degraded) of MMP9 associated with inflammation
4) Confidence 0.61 Published 2010 Journal Clin Proteomics Section Body Doc Link PMC2970804 Disease Relevance 0.50 Pain Relevance 0.23
MMP-9 is considered to be a key determinant of extracellular matrix degradation, having collagen as the main substrate.
Protein_catabolism (degradation) of MMP-9 in extracellular matrix
5) Confidence 0.57 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2258002 Disease Relevance 1.14 Pain Relevance 0.31
This progress would rely on invadopodia which are membrane protrusions that localize enzymes required for ECM degradation, and MMP9 would be required in the initial steps of invadopodia formation [20].
Protein_catabolism (degradation) of MMP9
6) Confidence 0.52 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 1.70 Pain Relevance 0.07
Neutrophil-derived, MMP-9-mediated tissue degradation and the instructional role of MMP-9 in directing the inflammatory response are key, and perhaps critical, events in the etiology of chronic obstructive pulmonary disease (COPD) [38]; systemic and cerebral vascular diseases [39], asthma [2,5], and periodontitis[6].
Protein_catabolism (degradation) of MMP-9 in Neutrophil associated with asthma, inflammatory response, periodontitis, chronic obstructive pulmonary disease and increased venous pressure under development
7) Confidence 0.35 Published 2008 Journal BMC Cell Biol Section Body Doc Link PMC2375863 Disease Relevance 1.06 Pain Relevance 0.26
Neutrophil-derived, MMP-9-mediated tissue degradation and the instructional role of MMP-9 in directing the inflammatory response are key, and perhaps critical, events in the etiology of chronic obstructive pulmonary disease (COPD) [38]; systemic and cerebral vascular diseases [39], asthma [2,5], and periodontitis[6].
Protein_catabolism (degradation) of MMP-9-mediated in Neutrophil associated with asthma, inflammatory response, periodontitis, chronic obstructive pulmonary disease and increased venous pressure under development
8) Confidence 0.35 Published 2008 Journal BMC Cell Biol Section Body Doc Link PMC2375863 Disease Relevance 1.05 Pain Relevance 0.23
Those results indicate an important contribution of mmp-9 to neovascularization of expanding bone metastases and to subsequent bone degradation.
Protein_catabolism (degradation) of mmp-9 associated with metastasis
9) Confidence 0.26 Published 2008 Journal Current Oncology Section Body Doc Link PMC2528310 Disease Relevance 1.42 Pain Relevance 0
Interestingly, CD44 may act as a tumor cell surface anchor for MMP-9, a matrix metalloproteinase, which may contribute to collagen degradation and contribute to tumor invasiveness [60]. sCD44 can disrupt CD44/MMP-9 clusters and inhibit tumor metastasis in vivo [60].
Protein_catabolism (degradation) of MMP-9 associated with cancer, metalloproteinase and metastasis
10) Confidence 0.23 Published 2003 Journal Tob Induc Dis Section Body Doc Link PMC2669563 Disease Relevance 1.10 Pain Relevance 0.05
Interestingly, CD44 may act as a tumor cell surface anchor for MMP-9, a matrix metalloproteinase, which may contribute to collagen degradation and contribute to tumor invasiveness [60]. sCD44 can disrupt CD44/MMP-9 clusters and inhibit tumor metastasis in vivo [60].
Protein_catabolism (degradation) of MMP-9 associated with cancer, metalloproteinase and metastasis
11) Confidence 0.23 Published 2003 Journal Tob Induc Dis Section Body Doc Link PMC2671531 Disease Relevance 1.10 Pain Relevance 0.05
Although mmp-9 does not degrade type i collagen, the most abundant organic component in bone, we found that the protease is expressed mainly by osteoclasts.
Neg (not) Protein_catabolism (degrade) of mmp-9 in osteoclasts
12) Confidence 0.22 Published 2008 Journal Current Oncology Section Body Doc Link PMC2528310 Disease Relevance 0.90 Pain Relevance 0

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