INT123839

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.15
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 6
Disease Relevance 4.69
Pain Relevance 1.21

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

extracellular space (Timp2) aging (Timp2) extracellular region (Timp2)
nucleus (Timp2)
Anatomy Link Frequency
ECM 2
brain 1
Timp2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 19 100.00 Very High Very High Very High
cytokine 39 99.60 Very High Very High Very High
ischemia 17 99.02 Very High Very High Very High
Restless leg syndrome 1 96.98 Very High Very High Very High
tolerance 16 89.48 High High
fibrosis 11 80.00 Quite High
Inflammation 19 79.52 Quite High
anesthesia 2 70.72 Quite High
halothane 2 70.28 Quite High
Angina 4 14.00 Low Low
Disease Link Frequency Relevance Heat
Diabetic Cardiomyopathies 105 99.72 Very High Very High Very High
Diabetes Mellitus 205 99.32 Very High Very High Very High
Cv General 4 Under Development 6 99.02 Very High Very High Very High
Cv Unclassified Under Development 11 98.52 Very High Very High Very High
Acute Coronary Syndrome 1 98.52 Very High Very High Very High
Peripheral Arterial Disease 4 98.00 Very High Very High Very High
Increased Venous Pressure Under Development 6 96.98 Very High Very High Very High
Injury 79 94.16 High High
Pressure And Volume Under Development 32 92.72 High High
Stroke 5 90.80 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
It was postulated that this was because of destruction or neutralization of the cytokines by tissue and bacterial matrix metalloproteinases (MMPs).32 One reason that ACCS may have been effective in this model in physiological doses of cytokines is because of high levels of TIMP-1 and TIMP-2, known natural inhibitors to MMPs.8 These high levels of TIMPs improve the MMP/TIMP ratio, which has been reported to improve healing in chronic wounds.33 Tissue bacterial bioburden remained high (>105 CFUs/g of tissue) in both treated and control wounds.
Positive_regulation (levels) of TIMP-2 associated with injury, metalloproteinase and cytokine
1) Confidence 0.15 Published 2008 Journal Eplasty Section Body Doc Link PMC2323202 Disease Relevance 0.72 Pain Relevance 0.28
There was an increase in TIMP-1, TIMP-2 and TGF-?
Positive_regulation (increase) of TIMP-2
2) Confidence 0.14 Published 2009 Journal Mol Biol Rep Section Body Doc Link PMC2831180 Disease Relevance 0.26 Pain Relevance 0
Also high levels of MMP-9 and TIMP-2 have been found in patients with an acute coronary syndrome and type 2 diabetes, probably reflecting an abnormal extracellular matrix metabolism in these patients [29].
Positive_regulation (levels) of TIMP-2 in extracellular matrix associated with acute coronary syndrome and diabetes mellitus
3) Confidence 0.11 Published 2010 Journal Cardiovasc Diabetol Section Body Doc Link PMC2940874 Disease Relevance 1.13 Pain Relevance 0.13
Paralleling these effects on cerebral ischemia, olmesartan treatment also reduced the reactive upregulation in brain angiotensin II, matrix metalloproteinase-2, matrix metalloproteinase-9, and membrane type 1-matrix metalloproteinase in the ischemic area.
Positive_regulation (upregulation) of metalloproteinase-2 in brain associated with cv general 4 under development, ischemia and metalloproteinase
4) Confidence 0.11 Published 2005 Journal Neuroscience Section Abstract Doc Link 15963646 Disease Relevance 1.11 Pain Relevance 0.57
We hypothesized that patients with intermittent claudication (with low ankle-brachial blood pressure index, <0.8), and critical ischaemia would have raised circulating levels of MMP-9, TIMP-1 and TIMP-2 compared with healthy controls, reflecting an increase in proteolytic activity which may be related to ECM turnover in PAD.
Positive_regulation (increase) of TIMP-2 in ECM associated with restless leg syndrome, cv unclassified under development and peripheral arterial disease
5) Confidence 0.07 Published 2005 Journal J. Intern. Med. Section Abstract Doc Link 15606382 Disease Relevance 0.61 Pain Relevance 0.14
These results suggest that O-glycosylation of protein modifies collagen expression and, therefore, contributes to DCM.170 ROSs play an important role in the development of DCM.42,43 Matrix metalloproteinase 2 (MMP-2) is activated by ROS and contributes to the acute loss of myocardial contractile function by targeting and cleaving susceptible proteins including troponin I and ?
Positive_regulation (activated) of metalloproteinase 2 associated with metalloproteinase and diabetic cardiomyopathies
6) Confidence 0.01 Published 2010 Journal Vascular Health and Risk Management Section Body Doc Link PMC2964943 Disease Relevance 0.87 Pain Relevance 0.09

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox