INT34487

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Context Info
Confidence 0.81
First Reported 1987
Last Reported 2010
Negated 0
Speculated 1
Reported most in Abstract
Documents 56
Total Number 57
Disease Relevance 31.41
Pain Relevance 23.61

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 (MMP2) extracellular space (MMP2) extracellular region (MMP2)
proteinaceous extracellular matrix (MMP2) plasma membrane (MMP2) nucleus (MMP2)
Anatomy Link Frequency
fibroblasts 4
THP-1 3
smooth muscle cells 3
HL-60 2
brain 2
MMP2 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 2062 100.00 Very High Very High Very High
cytokine 742 100.00 Very High Very High Very High
rheumatoid arthritis 612 100.00 Very High Very High Very High
ischemia 22 99.98 Very High Very High Very High
Nicotine 172 99.72 Very High Very High Very High
Inflammation 567 99.46 Very High Very High Very High
Morphine 32 99.42 Very High Very High Very High
tetrodotoxin 6 99.36 Very High Very High Very High
Snapping jaw 5 99.24 Very High Very High Very High
opiate 4 98.96 Very High Very High Very High
Disease Link Frequency Relevance Heat
Rheumatoid Arthritis 612 100.00 Very High Very High Very High
Cv Unclassified Under Development 42 99.98 Very High Very High Very High
Primary Sclerosing Cholangitis 44 99.96 Very High Very High Very High
Adhesions 451 99.90 Very High Very High Very High
Herpes Simplex Virus 2144 99.82 Very High Very High Very High
Disorders Of The Lacrimal System 1 99.68 Very High Very High Very High
Reprotox - General 1 6 99.48 Very High Very High Very High
INFLAMMATION 653 99.46 Very High Very High Very High
Infection 988 99.36 Very High Very High Very High
Temporomandibular Joint Syndrome 5 99.24 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Immunolocalization of gelatinase-A (matrix metalloproteinase-2) in damaged human temporomandibular joint discs.
Localization (Immunolocalization) of matrix metalloproteinase-2 in temporomandibular joint associated with snapping jaw and metalloproteinase
1) Confidence 0.81 Published 1999 Journal Arch. Oral Biol. Section Title Doc Link 10348355 Disease Relevance 0.54 Pain Relevance 0.34
NS398 also reduced the amount of MMP-2, not MMP-9, released into the medium.
Localization (released) of MMP-2
2) Confidence 0.76 Published 2001 Journal FEBS Lett. Section Abstract Doc Link 11728453 Disease Relevance 0.41 Pain Relevance 0.30
The expression and tissue immunolocalization of MMP-2 in fibrocartilages from these condyles was examined histochemically.
Spec (examined) Localization (immunolocalization) of MMP-2 in fibrocartilages associated with metalloproteinase
3) Confidence 0.71 Published 2000 Journal J. Oral Pathol. Med. Section Abstract Doc Link 10947247 Disease Relevance 0.52 Pain Relevance 0.52
RPN 2610, RPN 2617, RPN 2613, RPN 2614, RPN 2611, RPN 2618, RPN 2612) for the determination of MMP1, MMP2, MMP3, MMP9, TIMP1, TIMP2, and MTC1 concentrations in the blood plasma of the patients and the control group.
Localization (concentrations) of MMP2 in plasma
4) Confidence 0.70 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.12 Pain Relevance 0.05
It also lowered down the activity of MMP-2 and MMP-9, and could reduce of MMP-2 secretion of cell lines.
Localization (secretion) of MMP-2
5) Confidence 0.69 Published 2005 Journal J. Neurooncol. Section Abstract Doc Link 15803368 Disease Relevance 0.26 Pain Relevance 0
MMP-2 activity assay showed the total and active MMP-2 secretion was suppressed by 500 microM/ml of indomethacin.
Localization (secretion) of MMP-2
6) Confidence 0.69 Published 2005 Journal J. Neurooncol. Section Abstract Doc Link 15803368 Disease Relevance 0.36 Pain Relevance 0.14
Activated MMP1, MMP3 and latent forms of MMP2 and MMP9 are regulated and inhibited by endogenous proteins known as tissue inhibitors of metalloproteinase TIMP1 and TIMP2 [17].
Localization (forms) of MMP2 associated with metalloproteinase
7) Confidence 0.66 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.82 Pain Relevance 0.23
Gelatinase release induced by fMet-Leu-Phe was affected to the same extent, or slightly more, than release of the other granule enzymes.
Localization (release) of Gelatinase
8) Confidence 0.63 Published 1987 Journal Biochem. Pharmacol. Section Abstract Doc Link 3038127 Disease Relevance 0.15 Pain Relevance 0.15
With immune complexes, there was only modest inhibition of gelatinase release by any of the drugs at 250-1000 microM.
Localization (release) of gelatinase
9) Confidence 0.55 Published 1987 Journal Biochem. Pharmacol. Section Abstract Doc Link 3038127 Disease Relevance 0.17 Pain Relevance 0.17
Cytochrome c reduction and the release of lysozyme, beta-glucuronidase, myeloperoxidase and gelatinase were measured.
Localization (release) of gelatinase
10) Confidence 0.55 Published 1987 Journal Biochem. Pharmacol. Section Abstract Doc Link 3038127 Disease Relevance 0.17 Pain Relevance 0.12
Although the exact cellular source of MMPs remains unknown, brain endothelium, astrocytes, neurons, and inflammatory-activated cells, such as neutrophils, may release MMP-2, MMP-3, MMP-8, MMP-9, MMP-10, and/or MMP-13.
Localization (release) of MMP-2 in brain associated with inflammation and metalloproteinase
11) Confidence 0.45 Published 2010 Journal Ann. N. Y. Acad. Sci. Section Abstract Doc Link 20955435 Disease Relevance 1.06 Pain Relevance 0.52
Thus, aeroplysinin-1 seems to affect mainly the release of MMP-2 to the medium [64].


Localization (release) of MMP-2
12) Confidence 0.40 Published 2009 Journal Marine Drugs Section Body Doc Link PMC2707034 Disease Relevance 0.16 Pain Relevance 0.07
By exploiting the cartilage explant culture, p-hydroxycinnamaldehyde suppressed loss of uronic acid, resulting in release of hyaluronan (HA), sulfated glycosaminoglycans (s-GAGs) and matrix metalloproteinases (MMPs). p-Hydroxycinnamaldehyde and interleukin-1beta (IL-1beta), when incubated in primary human chondrocytes, also reduced release of HA, s-GAG and MMP-2.
Localization (release) of MMP-2 in chondrocytes associated with metalloproteinase
13) Confidence 0.39 Published 2009 Journal Phytochemistry Section Abstract Doc Link 19118849 Disease Relevance 0.29 Pain Relevance 0.35
Concomitantly, cannabinoid receptor activation specifically decreased invasiveness of PSC, MMP-2 secretion and led to changes in PSC phenotype accompanied by a reduction of intracellular stress fibres.


Localization (secretion) of MMP-2 associated with stress, cannabinoid receptor and primary sclerosing cholangitis
14) Confidence 0.36 Published 2008 Journal PLoS ONE Section Abstract Doc Link PMC2253501 Disease Relevance 1.16 Pain Relevance 0.97
The gel zymography results show that MMP-9 and MMP-2 secretion increased significantly in the co-culture of isolated human CD14+ monocytes and fibroblasts for both the RA and normal control groups compared with the cultures of human monocytes or fibroblasts alone (Fig. 4).
Localization (secretion) of MMP-2 in fibroblasts associated with rheumatoid arthritis and metalloproteinase
15) Confidence 0.36 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.68 Pain Relevance 0.88
AP9 had some inhibitory effect on the secretion of pro-MMP9 (control, 33.7 ± 18.5%; RA, 31.8 ± 16.2), MMP-9 (control, 41.9 ± 5.8%; RA, 43.8 ± 5.1%) and MMP-2 (control, 100%; RA, 63.9 ± 6.2%) in the co-culture of human monocytes and fibroblasts in both the normal control and RA groups (Fig. 4c).
Localization (secretion) of MMP-2 in monocytes associated with metalloproteinase and rheumatoid arthritis
16) Confidence 0.36 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.45 Pain Relevance 0.61
The pro-MMP-9, MMP-9 and MMP-2 secretion in the co-culture of differentiated THP-1 cells and fibroblasts decreased significantly (27.5 ± 12.7%, 25.4 ± 12.4% and 25.5 ± 3.8%, respectively) in the AP9 group compared with those without AP9 (p < 0.01; Fig. 5d).
Localization (secretion) of MMP-2 in fibroblasts associated with metalloproteinase
17) Confidence 0.36 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.40 Pain Relevance 0.59
Elevated secretion of pro-MMP-2 and MMP-2 was observed in the co-culture of differentiated THP-1 cells and fibroblasts (Fig. 5b).


Localization (secretion) of MMP-2 in THP-1 associated with metalloproteinase
18) Confidence 0.36 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.39 Pain Relevance 0.64
1 integrin receptors and the subsequent induction of MMP-2 secretion.
Localization (secretion) of MMP-2
19) Confidence 0.36 Published 2010 Journal Obstetrics and Gynecology International Section Body Doc Link PMC2913851 Disease Relevance 0.96 Pain Relevance 0
The co-culture of undifferentiated THP-1 cells and fibroblasts showed a significantly elevated level of release and activation of MMP-2 and particularly MMP-9 compared with the cultures of THP-1 cells or fibroblasts alone (Fig. 5a).
Localization (release) of MMP-2 in THP-1 associated with metalloproteinase
20) Confidence 0.34 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257431 Disease Relevance 0.28 Pain Relevance 0.70

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