INT103210

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Context Info
Confidence 0.78
First Reported 2002
Last Reported 2011
Negated 1
Speculated 0
Reported most in Body
Documents 43
Total Number 43
Disease Relevance 12.15
Pain Relevance 15.13

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 (MMP1) extracellular region (MMP1) proteinaceous extracellular matrix (MMP1)
Anatomy Link Frequency
fibroblasts 16
synovial fluid 2
plasma 1
stroma 1
macrophages 1
MMP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 2076 100.00 Very High Very High Very High
rheumatoid arthritis 58 99.56 Very High Very High Very High
Osteoarthritis 181 99.48 Very High Very High Very High
cytokine 196 99.08 Very High Very High Very High
pulpitis 12 98.28 Very High Very High Very High
COX2 16 95.68 Very High Very High Very High
Inflammation 195 94.52 High High
chemokine 60 89.92 High High
cOX1 1 89.16 High High
Arthritis 17 88.64 High High
Disease Link Frequency Relevance Heat
Rheumatoid Arthritis 58 99.56 Very High Very High Very High
Osteoarthritis 185 99.48 Very High Very High Very High
Pulpitis 12 98.28 Very High Very High Very High
Bladder Cancer 145 98.20 Very High Very High Very High
Transitional Cell Carcinoma 130 96.24 Very High Very High Very High
Pre-term Labor 91 96.08 Very High Very High Very High
Injury 40 94.56 High High
INFLAMMATION 214 94.52 High High
Arthritis 61 94.24 High High
Stress 12 93.84 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
On the basis of the concept that MMPs are synthesized in tissue and released into the blood stream we evaluated the levels of MMPs, their inhibitors, and MTC1 in blood plasma from patients with TCC of the bladder at different grades, stages, and with and without metastasis.
Localization (released) of MMP in blood associated with metalloproteinase, metastasis and transitional cell carcinoma
1) Confidence 0.78 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.95 Pain Relevance 0.21
MMPs are also involved in the regulation of cell behaviour via the release of growth factors and cytokines from the substrates they cleave, increasing the magnitude of their effects.
Localization (release) of MMP associated with metalloproteinase and cytokine
2) Confidence 0.73 Published 2009 Journal Curr Drug Targets Section Abstract Doc Link 19909233 Disease Relevance 0.45 Pain Relevance 0.50
The study revealed that the most highly expressed MMPs are located in the stroma, except MMP13, which was located in the epithelium.
Neg (except) Localization (located) of MMP in stroma associated with metalloproteinase
3) Confidence 0.73 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.86 Pain Relevance 0.21
MMP Matrix metalloproteinase
Localization (metalloproteinase) of MMP associated with metalloproteinase
4) Confidence 0.73 Published 2002 Journal BMC Genomics Section Body Doc Link PMC122098 Disease Relevance 0.20 Pain Relevance 0.23
Immunohistochemically, MMP-1 and MMP-3 were localized in the infiltrating neutrophils, macrophages, and extracellular matrix of the acute pulpitis group.
Localization (localized) of MMP-1 in extracellular matrix associated with pulpitis and metalloproteinase
5) Confidence 0.70 Published 2002 Journal J Endod Section Abstract Doc Link 12043871 Disease Relevance 0.38 Pain Relevance 0.77
Since MMPs and TIMPs are released from platelets and leukocytes into serum during blood collections [21] plasma should be used to determine circulating MMPs and TIMPs [22,23].
Localization (released) of MMP in leukocytes associated with metalloproteinase
6) Confidence 0.68 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.63 Pain Relevance 0.51
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 MMP1 in plasma
7) Confidence 0.61 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.12 Pain Relevance 0.05
Consistent with quantitative real-time PCR findings, the ELISA assay demonstrated that levels of MMP-1 and MMP-13 protein secreted into the media were significantly decreased by 10 mmol/l glucosamine (P < 0.05; Figure 1c,d).
Localization (secreted) of MMP-1
8) Confidence 0.57 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212570 Disease Relevance 0 Pain Relevance 0.03
Levels of MMP-1 and MMP-3 secretion induced by IL-1?
Localization (secretion) of MMP-1
9) Confidence 0.57 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212570 Disease Relevance 0 Pain Relevance 0.04
LPS-induced IL-6 and PGE2 release was only slightly inhibited at high doses, whereas LPS-induced release of IL-8 and matrix metalloprotease (MMP)-9 was not affected.
Localization (release) of matrix metalloprotease
10) Confidence 0.46 Published 2004 Journal Scand. J. Rheumatol. Suppl. Section Abstract Doc Link 15515409 Disease Relevance 0.49 Pain Relevance 0.19
IL-1 beta also stimulated MMP-1 and -3 protein secretion.
Localization (secretion) of MMP-1
11) Confidence 0.40 Published 2003 Journal J. Orthop. Res. Section Abstract Doc Link 12568957 Disease Relevance 0.30 Pain Relevance 0.57
One interesting finding of this study is that preterm and term cervical fibroblasts show different secretion patterns of IL-8, MMP-1 and MMP-3, where IL-8 and MMP-1 are secreted at higher levels in preterm and MMP-3 in term cervical fibroblasts.
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
12) Confidence 0.36 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0 Pain Relevance 0.44
The clinical significance of different secretion patterns of IL-8, MMP-1 and MMP3 in preterm and term cervical fibroblasts still needs to be elucidated.
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
13) Confidence 0.36 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0 Pain Relevance 0.61
One interesting finding of this study is that preterm and term cervical fibroblasts show different secretion patterns of IL-8, MMP-1 and MMP-3, where IL-8 and MMP-1 are secreted at higher levels in preterm and MMP-3 in term cervical fibroblasts.
Localization (secreted) of MMP-1 in fibroblasts associated with metalloproteinase
14) Confidence 0.36 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0 Pain Relevance 0.43
The results on the secretion of MMP-1 and MMP-3 from cervical fibroblasts contradict the findings by Li and Challis (2005).
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
15) Confidence 0.33 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0 Pain Relevance 0.38
Furthermore, preterm and term cervical fibroblasts showed different secretion patterns of IL-8, MMP-1 and MMP-3.
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
16) Confidence 0.33 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0 Pain Relevance 0.74
The secretion of IL-8 and MMP-1 was higher in the preterm cervical fibroblasts (P < 0.001 and <0.05, respectively).
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
17) Confidence 0.31 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0.06 Pain Relevance 0.64
We have shown that CRH increased the secretion of IL-8 in both preterm and term cervical fibroblasts, but did not affect the secretion of MMP-1 and MMP-3.
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
18) Confidence 0.31 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0.08 Pain Relevance 0.42
Different secretion patterns of matrix metalloproteinases and IL-8 and effect of corticotropin-releasing hormone in preterm and term cervical fibroblasts

The aims of the present study were to compare the levels of mRNA and protein expression of matrix metalloproteinase (MMP)-1, -3, -8 and -9 in human cervical tissue in preterm and term labor as well as not in labor and to determine if corticotropin-releasing hormone (CRH) has an effect on MMP-1, -3 and interleukin (IL)-8 secretion in both preterm and term cervical fibroblasts.

Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
19) Confidence 0.31 Published 2008 Journal Molecular Human Reproduction Section Title Doc Link PMC2639405 Disease Relevance 0.16 Pain Relevance 0.37
However, different secretion patterns of IL-8, MMP-1 and MMP-3 in preterm and term cervical fibroblasts indicate that they might have different phenotypes.
Localization (secretion) of MMP-1 in fibroblasts associated with metalloproteinase
20) Confidence 0.31 Published 2008 Journal Molecular Human Reproduction Section Body Doc Link PMC2639405 Disease Relevance 0 Pain Relevance 0.25

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