INT94433

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Context Info
Confidence 0.55
First Reported 2001
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 16
Total Number 17
Disease Relevance 9.38
Pain Relevance 4.78

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular region (TIMP2)
Anatomy Link Frequency
spinal 1
cartilage 1
endometrium 1
TIMP2 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 219 100.00 Very High Very High Very High
endometriosis 168 99.86 Very High Very High Very High
Dismenorea 20 99.08 Very High Very High Very High
rheumatoid arthritis 253 98.84 Very High Very High Very High
cocaine 59 98.66 Very High Very High Very High
spinal stenosis 44 97.60 Very High Very High Very High
medulla 2 89.40 High High
Arthritis 20 87.28 High High
Catecholamine 10 83.60 Quite High
cytokine 58 77.64 Quite High
Disease Link Frequency Relevance Heat
Endometriosis 224 99.86 Very High Very High Very High
Cancer 235 99.48 Very High Very High Very High
Dysmenorrhea 16 99.08 Very High Very High Very High
Rheumatoid Arthritis 253 98.84 Very High Very High Very High
Spinal Stenosis 46 97.60 Very High Very High Very High
Disease 55 97.20 Very High Very High Very High
Poisoning 2 95.84 Very High Very High Very High
Pancreatic Cancer 1 95.60 Very High Very High Very High
Melanoma 88 94.16 High High
Primary Sclerosing Cholangitis 77 93.44 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
1), tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) and TIMP-2 in hypertrophied ligamentum flavum of patients with lumbar spinal stenosis compared to patients with lumbar disc herniation.
Negative_regulation (inhibitor) of TIMP-2 in spinal associated with metalloproteinase and spinal stenosis
1) Confidence 0.55 Published 2007 Journal Asian Spine Journal Section Body Doc Link PMC2857497 Disease Relevance 0.80 Pain Relevance 0.20
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].
Negative_regulation (inhibitors) of TIMP2 associated with metalloproteinase
2) Confidence 0.50 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.85 Pain Relevance 0.22
1), tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) and TIMP-2 were measured by enzyme-linked immunosorbent assay.


Negative_regulation (inhibitor) of TIMP-2 associated with metalloproteinase
3) Confidence 0.40 Published 2007 Journal Asian Spine Journal Section Abstract Doc Link PMC2857497 Disease Relevance 0.37 Pain Relevance 0.16
Neutralization of TIMP-2 activity by antibodies from RA patients
Negative_regulation (Neutralization) of TIMP-2 associated with rheumatoid arthritis
4) Confidence 0.37 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257425 Disease Relevance 0.26 Pain Relevance 0.10
Indeed, TIMP-1 is a preferential inhibitor of soluble MMPs, while TIMP-2 and TIMP-3 are also efficient inhibitors of the membrane-bound MMPs.
Negative_regulation (inhibitors) of TIMP-2 associated with metalloproteinase
5) Confidence 0.37 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257425 Disease Relevance 0.28 Pain Relevance 0.51
Importantly, we showed that TIMP-2 antibodies purified from RA patients were functionally active, since they were able to neutralize TIMP-2-mediated inhibition of MMP9.
Negative_regulation (inhibition) of TIMP-2-mediated associated with rheumatoid arthritis
6) Confidence 0.37 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257425 Disease Relevance 0.77 Pain Relevance 0.29
Taking into consideration that TIMP-2 functions predominantly as an MMP9 inhibitor (through its catalytic domain) and a proMMP2 activator (through its noncatalytic haemopexin domain), the presence of anti-TIMP-2 antibodies may favour accumulation of functional MMP2.
Negative_regulation (inhibitor) of TIMP-2
7) Confidence 0.32 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257425 Disease Relevance 0.55 Pain Relevance 0.31
The major angiogenic proteins downregulated by celecoxib treatment were VEGF, GRO, IL-6, IL-8, TIMP1, and TIMP2 (Figure 5).
Negative_regulation (downregulated) of TIMP2
8) Confidence 0.26 Published 2006 Journal Breast Cancer Res Section Body Doc Link PMC1797025 Disease Relevance 0.41 Pain Relevance 0.06
In our study celecoxib was able to neutralize the inductive potential of the tumor cell microenvironment by decreasing levels of MMPs, TIMP1, TIMP2, and laminin (Figures 4 and 5).
Negative_regulation (decreasing) of TIMP2 associated with cancer and metalloproteinase
9) Confidence 0.26 Published 2006 Journal Breast Cancer Res Section Body Doc Link PMC1797025 Disease Relevance 0.46 Pain Relevance 0.14
The cell culture supernatants of vehicle treated cells had greater amounts of growth related protein (GRO), IL-6, IL-8, tissue inhibitor of matrix metalloproteinase (TIMP)1 and TIMP2, and VEGF, based on gray levels or brightness values as compared with cells treated with celecoxib.
Negative_regulation (inhibitor) of TIMP2 associated with metalloproteinase
10) Confidence 0.26 Published 2006 Journal Breast Cancer Res Section Body Doc Link PMC1797025 Disease Relevance 0 Pain Relevance 0.10
Polymorphisms in the matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 and the risk of human adenomyosis.
Negative_regulation (inhibitor) of metalloproteinase-2 associated with dismenorea and metalloproteinase
11) Confidence 0.21 Published 2008 Journal Environ. Mol. Mutagen. Section Title Doc Link 18288718 Disease Relevance 0.42 Pain Relevance 0.61
Polymorphisms in the matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 and the risk of human adenomyosis.
Negative_regulation (inhibitor) of metalloproteinase-2 associated with dismenorea and metalloproteinase
12) Confidence 0.21 Published 2008 Journal Environ. Mol. Mutagen. Section Title Doc Link 18288718 Disease Relevance 0.41 Pain Relevance 0.61
S100A4 may mediate invasive potential by regulating matrix metalloproteinases and tissue inhibitors of matrix metalloproteinases such as TIMP2 [31].
Negative_regulation (inhibitors) of TIMP2 associated with metalloproteinase
13) Confidence 0.18 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2794539 Disease Relevance 1.35 Pain Relevance 0.14
Furthermore, the matrix degradation enzyme MMP-1 was induced (LPS by 46%; TNFalpha by 454%), while its inhibitor TIMP-2 was suppressed (by 20% and 18%, respectively; data not shown).
Negative_regulation (suppressed) of TIMP-2
14) Confidence 0.12 Published 2007 Journal J Transl Med Section Body Doc Link PMC2234395 Disease Relevance 0.60 Pain Relevance 0.04
CTS also counteracted cartilage degradation by augmenting expression of mRNA for tissue inhibitor of metalloproteinases 2 that is inhibited by rHuIL-1beta.
Negative_regulation (inhibitor) of metalloproteinases 2 in cartilage
15) Confidence 0.05 Published 2001 Journal Arthritis Rheum. Section Body Doc Link 11263775 Disease Relevance 0 Pain Relevance 0
In contrast, another study reported MMP-1 and MMP-2 to be highly expressed in eutopic but not ectopic endometrium of women with endometriosis and a decrease in the MMP-2 inhibitor (TIMP-2) [98], suggesting a role of MMP in the very early development of the disease.
Negative_regulation (decrease) of TIMP-2 in endometrium associated with endometriosis, metalloproteinase and disease
16) Confidence 0.05 Published 2007 Journal Semin Immunopathol Section Body Doc Link PMC2668599 Disease Relevance 0.97 Pain Relevance 0.70
There is evidence that cocaine may enhance the renal cortical messenger RNA expression of tissue inhibitors of metalloproteinase-2 [8].
Negative_regulation (inhibitors) of metalloproteinase-2 associated with metalloproteinase and cocaine
17) Confidence 0.02 Published 2005 Journal BMC Nephrol Section Body Doc Link PMC1253515 Disease Relevance 0.88 Pain Relevance 0.60

General Comments

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