INT102158

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Context Info
Confidence 0.65
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 7
Total Number 7
Disease Relevance 5.43
Pain Relevance 1.91

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) aging (Mmp9)
extracellular region (Mmp9) proteinaceous extracellular matrix (Mmp9) extracellular matrix organization (Mmp9)
Anatomy Link Frequency
extracellular matrix 3
cartilage 1
brain 1
Schwann cells 1
Mmp9 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 85 100.00 Very High Very High Very High
ischemia 35 99.28 Very High Very High Very High
Demyelination 1 98.84 Very High Very High Very High
Pain 37 90.28 High High
Inflammation 8 86.36 High High
Sciatic nerve 1 81.64 Quite High
Eae 1 80.80 Quite High
Osteoarthritis 33 66.56 Quite High
Peripheral nerve injury 1 62.24 Quite High
Neuronal nitric oxide synthase 1 61.72 Quite High
Disease Link Frequency Relevance Heat
Cv Unclassified Under Development 22 99.28 Very High Very High Very High
Glioma 24 98.96 Very High Very High Very High
Demyelinating Disease 1 98.84 Very High Very High Very High
Stroke 100 97.80 Very High Very High Very High
Death 6 97.56 Very High Very High Very High
Diabetes Mellitus 91 97.52 Very High Very High Very High
Cancer 45 96.60 Very High Very High Very High
Pressure And Volume Under Development 13 96.48 Very High Very High Very High
Brain Injury 4 92.84 High High
Pain 33 90.28 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
MMP-9 is a protease that degrades extracellular matrix and promotes BBB breakdown.
Protein_catabolism (degrades) of MMP-9 in extracellular matrix
1) Confidence 0.65 Published 2010 Journal BMC Genomics Section Body Doc Link PMC2875237 Disease Relevance 0.70 Pain Relevance 0.04
The reduction in chondropathy scores is likely due to a direct effect of the MMPi on proteinases, such as collagenase 3 or MMP9, that can degrade cartilage matrix proteins.
Protein_catabolism (degrade) of MMP9 in cartilage
2) Confidence 0.55 Published 2010 Journal Osteoarthritis and Cartilage Section Body Doc Link PMC2853084 Disease Relevance 0.71 Pain Relevance 0.62
Another study reported increased MMP-2 and MMP-9 activity and rapid degradation of occludin after temporary focal ischemia (38).
Protein_catabolism (degradation) of MMP-9 associated with ischemia and metalloproteinase
3) Confidence 0.54 Published 2010 Journal Diabetes Section Body Doc Link PMC2797926 Disease Relevance 0.95 Pain Relevance 0.20
TNF co-localized with myelin degrading MMP-9 within Schwann cells during demyelination, and intraaxonally during remyelination.
Protein_catabolism (degrading) of MMP-9 in Schwann cells associated with demyelination and metalloproteinase
4) Confidence 0.47 Published 2002 Journal J. Peripher. Nerv. Syst. Section Abstract Doc Link 11939349 Disease Relevance 0.85 Pain Relevance 0.76
Since MMP-2 and MMP-9 are believed to be largely responsible for the degradation of the blood brain barrier and also involved in the signaling of neuronal cell death [24,25], the inhibition of the proteolytic cascade is a logical target for several models of brain injury that involve matrix degradation and vascular instability [26].
Protein_catabolism (degradation) of MMP-9 in brain associated with brain injury and death
5) Confidence 0.46 Published 2006 Journal BMC Neurosci Section Body Doc Link PMC1543649 Disease Relevance 0.95 Pain Relevance 0.14
More recent studies have shown that NO generated from iNOS activity modulates the expression of matrix metalloproteinase-9 (MMP-9), an enzyme responsible for degradation of extracellular matrix, which significantly influenced cell migration [21].
Protein_catabolism (degradation) of MMP-9 in extracellular matrix associated with metalloproteinase
6) Confidence 0.30 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2797399 Disease Relevance 0.06 Pain Relevance 0.11
In order for angiogenesis to progress extracellular matrix (ECM) degradation is necessary and the metalloproteinases 2 and 9 (MMP2 and MMP9) are highly expressed in gliomas [19,20].
Protein_catabolism (degradation) of MMP9 in extracellular matrix associated with metalloproteinase and glioma
7) Confidence 0.30 Published 2009 Journal Lipids Health Dis Section Body Doc Link PMC2661078 Disease Relevance 1.22 Pain Relevance 0.05

General Comments

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