INT34232

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Context Info
Confidence 0.61
First Reported 1987
Last Reported 2010
Negated 6
Speculated 2
Reported most in Body
Documents 37
Total Number 41
Disease Relevance 18.76
Pain Relevance 6.05

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

aging (TIMP1) extracellular region (TIMP1)
Anatomy Link Frequency
plasma 2
fibroblasts 2
blood 2
monocyte 2
extracellular matrix 2
TIMP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 450 100.00 Very High Very High Very High
Dismenorea 3 99.82 Very High Very High Very High
cINOD 19 99.08 Very High Very High Very High
fibrosis 25 96.80 Very High Very High Very High
rheumatoid arthritis 427 95.52 Very High Very High Very High
Inflammation 375 93.88 High High
Arthritis 195 92.60 High High
Central nervous system 4 84.40 Quite High
depression 61 81.00 Quite High
methotrexate 23 78.72 Quite High
Disease Link Frequency Relevance Heat
Dysmenorrhea 3 99.82 Very High Very High Very High
Disease 428 99.52 Very High Very High Very High
Myocardial Infarction 88 98.96 Very High Very High Very High
INFLAMMATION 428 98.88 Very High Very High Very High
Schizophrenia 69 98.76 Very High Very High Very High
Hemorrhage 6 98.38 Very High Very High Very High
Transitional Cell Carcinoma 130 98.00 Very High Very High Very High
Fibrosis 41 96.80 Very High Very High Very High
Major Depressive Disorder 25 95.88 Very High Very High Very High
Rheumatoid Arthritis 430 95.52 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Uncoordinate regulation of collagenase, stromelysin, and tissue inhibitor of metalloproteinases genes by prostaglandin E2: selective enhancement of collagenase gene expression in human dermal fibroblasts in culture.
Regulation (regulation) of collagenase in fibroblasts associated with metalloproteinase
1) Confidence 0.61 Published 1994 Journal J. Cell. Biochem. Section Title Doc Link 8014195 Disease Relevance 0.14 Pain Relevance 0.23
Analysis of the intracellular regulation of collagenase revealed that synthesis of this enzyme required a prostaglandin (PGE2)-dependent step since indomethacin-inhibited enzyme synthesis was reversed by PGE2.
Regulation (regulation) of collagenase
2) Confidence 0.60 Published 1987 Journal Cell. Immunol. Section Abstract Doc Link 3032463 Disease Relevance 0.21 Pain Relevance 0.20
In media conditioned by chorion, the initiation of uterine contractions did not change MMP activity or TIMP-1 levels.
Neg (not) Regulation (change) of TIMP-1 in chorion associated with dismenorea
3) Confidence 0.58 Published 2003 Journal Mol. Hum. Reprod. Section Abstract Doc Link 12771238 Disease Relevance 0.35 Pain Relevance 0.40
Given that fibrinogen is a substrate of MMP9 [39–41], it is possible that up regulation of MMP9 and TIMP1 in circulation may be directly associated to the generation of FGA peptide biomarkers that ultimately are enriched in urine during active SJIA.
Regulation (regulation) of TIMP1 in urine
4) Confidence 0.54 Published 2010 Journal Clin Proteomics Section Body Doc Link PMC2970804 Disease Relevance 0.63 Pain Relevance 0.21
Uncoordinate regulation of collagenase, stromelysin, and tissue inhibitor of metalloproteinases genes by prostaglandin E2: selective enhancement of collagenase gene expression in human dermal fibroblasts in culture.
Regulation (regulation) of metalloproteinases in fibroblasts associated with metalloproteinase
5) Confidence 0.53 Published 1994 Journal J. Cell. Biochem. Section Title Doc Link 8014195 Disease Relevance 0.14 Pain Relevance 0.24
Regulation of human peripheral blood monocyte collagenase by prostaglandins and anti-inflammatory drugs.
Regulation (Regulation) of collagenase in monocyte associated with inflammation and cinod
6) Confidence 0.52 Published 1987 Journal Cell. Immunol. Section Title Doc Link 3032463 Disease Relevance 0.19 Pain Relevance 0.15
Ivy bleeding time was prolonged, but other hemostaseologic parameters were not significantly altered, after four weeks of 3.4 g/day EPA–DHA in 40 patients after myocardial infarction (Smith et al 1989).
Neg (not) Regulation (altered) of EPA associated with hemorrhage and myocardial infarction
7) Confidence 0.37 Published 2006 Journal Vascular Health and Risk Management Section Body Doc Link PMC1993981 Disease Relevance 0.96 Pain Relevance 0.04
For schizophrenic patients, docosahexaenoic acid (DHA) supplements inhibit the effects of EPA supplements so it is recommended that the patient only takes the EPA supplement, which the body will convert into the amount DHA it needs [59-65].
Regulation (effects) of EPA in body associated with schizophrenia
8) Confidence 0.37 Published 2008 Journal Nutr J Section Body Doc Link PMC2248201 Disease Relevance 1.12 Pain Relevance 0.03
These include paracellular permeability (down-regulation of OCLN) [54], degradation of extracellular matrix (up-regulation of TIMP and MMP2) [55,56] and barrier protection against bacterial invasion of the epithelial surface (up-regulation of MUC1) [57].
Regulation (regulation) of TIMP in extracellular matrix
9) Confidence 0.34 Published 2005 Journal PLoS Medicine Section Body Doc Link PMC1188246 Disease Relevance 1.36 Pain Relevance 0.05
Since tissue macrophages are derived from circulating peripheral blood monocytes, we used these less-differentiated, more readily available cells to examine the production and regulation of collagenase.
Spec (examine) Regulation (regulation) of collagenase in monocytes
10) Confidence 0.26 Published 1987 Journal Cell. Immunol. Section Abstract Doc Link 3032463 Disease Relevance 0.17 Pain Relevance 0.12
The role of TIMP-1 in the anti-invasive action of cannabinoids was analyzed by transfecting HeLa, human cervical carcinoma (C33A), or human lung carcinoma cells (A549) cells with siRNA targeting TIMP-1.
Regulation (targeting) of TIMP-1 in A549
11) Confidence 0.26 Published 2008 Journal J. Natl. Cancer Inst. Section Body Doc Link 18159069 Disease Relevance 0.06 Pain Relevance 0
The plasma concentration of MMP2 was significantly higher in comparison to the control group whereas the concentrations of MMP1, TIMP1, TIMP2, and MTC1 were significantly lower from patients with non-metastasized TCC of the bladder in comparison to the healthy control group (Table I).
Regulation (concentrations) of TIMP1 in bladder associated with transitional cell carcinoma
12) Confidence 0.26 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.64 Pain Relevance 0.19
In this study the concentrations of MMP1, MMP2, MMP3, MMP9, their inhibitors TIMP1, TIMP2, and the MMP1/TIMP1-complex (MTC1) were quantified in blood plasma with the sandwich enzyme-linked immunosorbent assay (ELISA).
Regulation (concentrations) of TIMP1 in blood
13) Confidence 0.26 Published 2006 Journal BMC Urol Section Abstract Doc Link PMC1560390 Disease Relevance 0.44 Pain Relevance 0.13
Considering the effect of histological grading on the MMP and TIMP levels, only MMP1 differed between grade 1 and 2 (median 4.4 vs. 1.9, p = 0.006) while the concentrations of all parameters were independent of the histolological grade (p = 0.101 – 0.532).
Regulation (effect) of TIMP
14) Confidence 0.26 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 0.58 Pain Relevance 0.06
The concentrations of TIMP1, TIMP2, and MTC1 in plasma probes were significantly lower from patients with non-metastasized TCC compared to the controls.
Regulation (concentrations) of TIMP1 in plasma
15) Confidence 0.26 Published 2006 Journal BMC Urol Section Abstract Doc Link PMC1560390 Disease Relevance 0.35 Pain Relevance 0.03
In this study the concentrations of MMP1, MMP2, MMP3, MMP9, their inhibitors TIMP1, TIMP2, and the MMP1/TIMP1-complex (MTC1) were quantified in blood plasma with the sandwich enzyme-linked immunosorbent assay (ELISA).
Regulation (concentrations) of TIMP1 in blood
16) Confidence 0.26 Published 2006 Journal BMC Urol Section Abstract Doc Link PMC1560390 Disease Relevance 0.44 Pain Relevance 0.13
on TIMP are also ambiguous [153], because the regulation of matrix metalloproteinase and TIMP may depend on different tissue domains (superficial versus deep cartilage layers) and may also vary for intracellular and extracellular digestion of collagen [146,152].
Regulation (regulation) of TIMP in cartilage associated with metalloproteinase
17) Confidence 0.24 Published 2000 Journal Arthritis Res Section Body Doc Link PMC130001 Disease Relevance 0.62 Pain Relevance 0.31
The antibody array plasma profiling identified an SJIA plasma flare signature consisting of tissue inhibitor of metalloproteinase-1 (TIMP1), interleukin (IL)-18, regulated upon activation, normal T cell expressed and secreted (RANTES), P-Selectin, MMP9, and L-Selectin.


Regulation (regulated) of TIMP1 in T cell associated with metalloproteinase
18) Confidence 0.24 Published 2010 Journal Clin Proteomics Section Abstract Doc Link PMC2970804 Disease Relevance 0.84 Pain Relevance 0.18
EPA design values generated from a network of air pollution monitoring sites, federal reference method (FRM) PM2.5 air pollution data from 2000, 2001, and 2002 were obtained from the U.S.
Regulation (values) of EPA
19) Confidence 0.22 Published 2005 Journal Environ Health Perspect Section Body Doc Link PMC1280392 Disease Relevance 1.40 Pain Relevance 0.06
Once again, HNE behaves in a different way since it affects neither the migration of human HSC/MFs nor the expression of MMPs (MMP-1 and MMP-2) [189], and, differently from O2•-, which has been reported to up-regulate TIMP-2 [335], it stimulates only TIMP-1 expression [189].


Regulation (regulate) of TIMP
20) Confidence 0.21 Published 2008 Journal Fibrogenesis Tissue Repair Section Body Doc Link PMC2584013 Disease Relevance 0.09 Pain Relevance 0.03

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