INT172689

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Context Info
Confidence 0.68
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 15
Total Number 17
Disease Relevance 5.52
Pain Relevance 3.32

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 3
basal lamina 3
cleavage 2
microglia 2
chondrocytes 1
Mmp3 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 160 100.00 Very High Very High Very High
cytokine 45 99.98 Very High Very High Very High
nMDA receptor 336 96.80 Very High Very High Very High
Spinal cord 151 96.08 Very High Very High Very High
Arthritis 32 95.36 Very High Very High Very High
Glutamate receptor 16 93.60 High High
Pain 23 92.60 High High
Inflammation 86 89.68 High High
rheumatoid arthritis 33 86.36 High High
Osteoarthritis 76 85.92 High High
Disease Link Frequency Relevance Heat
Apoptosis 82 99.84 Very High Very High Very High
Middle Cerebral Artery Infarction 8 97.88 Very High Very High Very High
Infection 180 97.52 Very High Very High Very High
Disease 123 96.80 Very High Very High Very High
Arthritis 36 95.36 Very High Very High Very High
Brain Disease 8 95.28 Very High Very High Very High
Pain 23 92.60 High High
Nociception 1 90.04 High High
INFLAMMATION 103 89.68 High High
Injury 66 87.44 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
MMP3 also known as 53 kD polypeptide, transin or stromelysin-1, a secreted protease, may facilitate neurite growth by dissolving the extracellular matrix of the basal lamina at the growing tip of the axon (see Table 4 for references).
Localization (secreted) of transin in basal lamina
1) Confidence 0.68 Published 2002 Journal BMC Neurosci Section Body Doc Link PMC139981 Disease Relevance 0.26 Pain Relevance 0.14
Importantly, it was demonstrated that the released and proteolytically activated MMP-3 acts as signaling molecule to activate microglia, which in turn might play a role in exacerbating degenerative human brain disorders, such as Parkinson's disease [32].
Localization (released) of MMP-3 in microglia associated with brain disease and disease
2) Confidence 0.67 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0.52 Pain Relevance 0.17
The intensive nuclear staining detected in our experiments is in agreement with data from different recent publications showing convincingly that MMP-3 is localized in the nucleus in different tissues and cultured cell types [19], [20].
Localization (localized) of MMP-3 in nucleus
3) Confidence 0.67 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.15
Double staining experiments using MMP-3-specific and PSD-95-specific antibodies showed that comparison of both immunoreactivities revealed only few overlapping puncta (Fig. 4, D–G), suggesting that most MMP-3 protein is localized at sites within dendrites distinct from PSD-95 containing synapses.
Localization (localized) of MMP-3 protein in synapses
4) Confidence 0.67 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.17
Indeed, more recently it was shown that activated MMP-3 is released from apoptotic neuronal cells.
Localization (released) of MMP-3 in neuronal associated with apoptosis
5) Confidence 0.67 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0.49 Pain Relevance 0.18
Interestingly, also the neuronal isoform of agrin is cleaved by MMP-3 in ischemic neuronal tissue of rats after transient middle cerebral artery occlusion [30].
Localization (cleaved) of MMP-3 in middle cerebral artery associated with middle cerebral artery infarction
6) Confidence 0.62 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0.24 Pain Relevance 0.20
MMP3 also known as 53 kD polypeptide, transin or stromelysin-1, a secreted protease, may facilitate neurite growth by dissolving the extracellular matrix of the basal lamina at the growing tip of the axon (see Table 4 for references).
Localization (secreted) of stromelysin-1 in basal lamina
7) Confidence 0.58 Published 2002 Journal BMC Neurosci Section Body Doc Link PMC139981 Disease Relevance 0.20 Pain Relevance 0.14
MMP3 also known as 53 kD polypeptide, transin or stromelysin-1, a secreted protease, may facilitate neurite growth by dissolving the extracellular matrix of the basal lamina at the growing tip of the axon (see Table 4 for references).
Localization (secreted) of MMP3 in basal lamina
8) Confidence 0.58 Published 2002 Journal BMC Neurosci Section Body Doc Link PMC139981 Disease Relevance 0.26 Pain Relevance 0.15
Thus, in the mature NR1 subunit a second MMP-3 cleavage site should be localized within the sequence P787-L790, most likely between T789 and L790.


Localization (localized) of MMP-3 in cleavage
9) Confidence 0.51 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0.18
The existence of a protein fragment of about 38 kDa seen upon Coomassie staining of separated MMP-3 cleavage products, which was not recognized by the anti-penta-His antibody, indicated that one MMP-3 cleavage site should be localized near the very carboxy-terminus of the S1S2 protein.
Localization (localized) of MMP-3 in cleavage
10) Confidence 0.51 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0 Pain Relevance 0
Future research will reveal by which cellular mechanisms the activity of MMP-3 is regulated and whether MMP-3 may be released at specific synaptic sites in order to allow local modifications of the perisynaptic network and of synaptic proteins like neuronal agrin and NMDA receptors, thereby contributing to increased synaptic plasticity.


Localization (released) of MMP-3 in neuronal associated with nmda receptor
11) Confidence 0.51 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2443283 Disease Relevance 0.49 Pain Relevance 0.34
Spinal p38 MAPK which then interacts with STAT4 or other molecules to induce signals that upregulate additional proinflammatory cytokine release such as IL-1, IL-6, or MMP3 in the periphery [4,7].
Localization (release) of MMP3 in Spinal associated with cytokine
12) Confidence 0.39 Published 2008 Journal J Neuroinflammation Section Body Doc Link PMC2235846 Disease Relevance 0.64 Pain Relevance 0.65
The release of MMP-3 was also attributed to neuronal cell degradation.
Localization (release) of MMP-3 in neuronal
13) Confidence 0.19 Published 2010 Journal BMC Infect Dis Section Body Doc Link PMC2915993 Disease Relevance 0.66 Pain Relevance 0.16
Our data show that concomitantly with the up-regulation of the microglia associated transcripts (CD68 and AIF-1), the released "On" signals matrix-metalloproteinase-3 (MMP-3) and CXCL10 are up-regulated in the acute phase (1 day after infection) of the disease, whereas the released "Off" signal CX3CL1 is down-regulated.
Localization (released) of MMP-3 in microglia associated with metalloproteinase, disease and infection
14) Confidence 0.16 Published 2010 Journal BMC Infect Dis Section Body Doc Link PMC2915993 Disease Relevance 0.47 Pain Relevance 0.12
Previous studies [47] showed that besides its involvement in the disruption of the blood brain barrier, MMP-3 is released by apoptotic neuronal cell lines and mediates the discharge of cytokines of contiguous microglial cells.
Localization (released) of MMP-3 in brain associated with apoptosis and cytokine
15) Confidence 0.16 Published 2010 Journal BMC Infect Dis Section Body Doc Link PMC2915993 Disease Relevance 0.66 Pain Relevance 0.17
In cultured chondrocytes, FGF8 induced the release of matrix metalloproteinase 3 and prostaglandin E2, and caused degradation of the ECM.
Localization (release) of matrix metalloproteinase 3 in chondrocytes associated with metalloproteinase
16) Confidence 0.15 Published 2008 Journal Arthritis Res Ther Section Abstract Doc Link PMC2575604 Disease Relevance 0.51 Pain Relevance 0.30
The effect of FGF8 on the release of proMMP-3 and PGE2 in the culture medium was investigated.
Localization (release) of proMMP-3
17) Confidence 0.15 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2575604 Disease Relevance 0.13 Pain Relevance 0.10

General Comments

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