INT93718

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Context Info
Confidence 0.73
First Reported 2000
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 9
Total Number 9
Disease Relevance 4.32
Pain Relevance 2.11

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 (Mmp3) extracellular space (Mmp3) extracellular region (Mmp3)
proteinaceous extracellular matrix (Mmp3) nucleus (Mmp3) protein complex (Mmp3)
Anatomy Link Frequency
neuronal 2
extracellular matrix 2
chondrocytes 1
joints 1
cleavage 1
Mmp3 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 81 100.00 Very High Very High Very High
nMDA receptor 127 99.68 Very High Very High Very High
intrathecal 37 96.32 Very High Very High Very High
Arthritis 47 94.92 High High
dorsal root ganglion 40 94.64 High High
cytokine 22 88.32 High High
Osteoarthritis 42 85.48 High High
allodynia 8 84.64 Quite High
Inflammatory response 8 78.16 Quite High
Inflammation 85 76.56 Quite High
Disease Link Frequency Relevance Heat
Death 13 99.48 Very High Very High Very High
Apoptosis 29 99.04 Very High Very High Very High
Ulcers 14 97.88 Very High Very High Very High
Nervous System Injury 83 95.40 Very High Very High Very High
Arthritis 32 94.92 High High
Ganglion Cysts 42 94.64 High High
Duodenal Ulcer 26 93.32 High High
Wound Healing 2 93.12 High High
Disease 43 90.92 High High
Infection 83 90.28 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, expression of a key gene involved with extracellular matrix degradation (MMP3) was also decreased (p = 0.001; Figure 3D).


Protein_catabolism (degradation) of MMP3 in extracellular matrix associated with metalloproteinase
1) Confidence 0.73 Published 2006 Journal PLoS Medicine Section Body Doc Link PMC1560929 Disease Relevance 0.43 Pain Relevance 0.65
As shown in Figure 3A, activated MMP-3 degraded solubilized NR1 subunits of about 110–120 kDa.
Protein_catabolism (degraded) of MMP-3
2) Confidence 0.64 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.16
Thus, matrix metallopeptidases 3 and 16, (MMP3 and MMP16) are proteoglycanases capable of degrading the major components of the extracellular matrix [53,54] and are related to macrophage invasion [55].
Protein_catabolism (degrading) of MMP3 in extracellular matrix
3) Confidence 0.54 Published 2009 Journal Mol Pain Section Body Doc Link PMC2799401 Disease Relevance 1.14 Pain Relevance 0.64
In addition, three amino acids arround serine 542 were replaced by different amino acid residues (see methods) because these P3-P1 positions are known to contribute to the specificity of MMP-3 cleavage [22].
Protein_catabolism (cleavage) of MMP-3 in cleavage
4) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0
Similarly, MMP-3 cleavage of the NMDA receptor NR1 subunit might be related to neuronal cell death.
Protein_catabolism (cleavage) of MMP-3 in neuronal associated with nmda receptor and death
5) Confidence 0.48 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0.64 Pain Relevance 0.19
The release of MMP-3 was also attributed to neuronal cell degradation.
Protein_catabolism (degradation) of MMP-3 in neuronal
6) Confidence 0.15 Published 2010 Journal BMC Infect Dis Section Body Doc Link PMC2915993 Disease Relevance 0.68 Pain Relevance 0.16
In cultured chondrocytes, FGF8 induced the release of matrix metalloproteinase 3 and prostaglandin E2, and caused degradation of the ECM.
Protein_catabolism (degradation) of matrix metalloproteinase 3 in chondrocytes associated with metalloproteinase
7) Confidence 0.14 Published 2008 Journal Arthritis Res Ther Section Abstract Doc Link PMC2575604 Disease Relevance 0.50 Pain Relevance 0.30
In general, MMP-3 can degrade a wide range of substrates, including fibronectin, type IV, V, IX, and X collagens, elastin, laminins, gelatin, and proteoglycan core proteins, and is thus helpful during wound healing of the skin [27-29].
Protein_catabolism (degrade) of MMP-3 in skin associated with wound healing
8) Confidence 0.10 Published 2010 Journal BMC Microbiol Section Body Doc Link PMC2928200 Disease Relevance 0.86 Pain Relevance 0
CONCLUSION: These findings suggest a strong association between the OA-active joints and the presence of biologically active forms of known tissue degradation enzymes (MMP-1, MMP-3, and MMP-9).


Protein_catabolism (degradation) of MMP-3 in joints
9) Confidence 0.04 Published 2000 Journal J Orofac Pain Section Body Doc Link 11203734 Disease Relevance 0.06 Pain Relevance 0

General Comments

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