INT58283

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Context Info
Confidence 0.23
First Reported 1993
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 8
Disease Relevance 6.07
Pain Relevance 2.08

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

transport (ABCC1) small molecule metabolic process (ABCC1) Golgi apparatus (ABCC1)
nucleolus (ABCC1) ATPase activity (ABCC1) plasma membrane (ABCC1)
Anatomy Link Frequency
renal tubule 1
erythrocytes 1
ABCC1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Angina 1 100.00 Very High Very High Very High
metalloproteinase 510 99.72 Very High Very High Very High
cytokine 386 99.44 Very High Very High Very High
Inflammation 201 98.24 Very High Very High Very High
chemokine 100 78.24 Quite High
COX-2 inhibitor 115 77.36 Quite High
cINOD 22 73.40 Quite High
rheumatoid arthritis 1 60.88 Quite High
Bioavailability 5 28.64 Quite Low
Inflammatory response 10 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Myocardial Infarction 1 100.00 Very High Very High Very High
Cv General 3 Under Development 1 100.00 Very High Very High Very High
Herpes Simplex Virus 1190 99.28 Very High Very High Very High
Coronary Artery Disease 4 98.84 Very High Very High Very High
INFLAMMATION 223 98.24 Very High Very High Very High
Sarcoma 395 96.32 Very High Very High Very High
Infection 520 96.04 Very High Very High Very High
Acquired Immune Deficiency Syndrome Or Hiv Infection 45 92.24 High High
Hepatitis B Virus Infection 5 91.68 High High
Hepatitis 5 91.16 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This drug is principally secreted into the urine via multidrug resistance protein (MRP) at proximal cells of renal tubule [26].
Localization (secreted) of multidrug resistance protein in renal tubule
1) Confidence 0.23 Published 2010 Journal AIDS Res Ther Section Body Doc Link PMC3020664 Disease Relevance 0.12 Pain Relevance 0
Experiments with radioactively-labeled 4OH-OPB suggest that 4OH-OPB is taken up very rapidly into erythrocytes and is secreted by the erythrocytes with much slower kinetics via a multidrug-resistance-associated protein.
Localization (secreted) of multidrug-resistance-associated protein in erythrocytes
2) Confidence 0.21 Published 2005 Journal Eur. Cytokine Netw. Section Abstract Doc Link 15941686 Disease Relevance 0.13 Pain Relevance 0.37
BACKGROUND: Excretion of leukotriene (LT) E4, the major urinary metabolite of cysteinyl leukotrienes in humans, is increased in patients with unstable angina and myocardial infarction, suggesting that cysteinyl leukotrienes are released into the circulation during episodes of myocardial ischaemia.
Localization (released) of leukotriene associated with angina, coronary artery disease and myocardial infarction
3) Confidence 0.07 Published 1993 Journal Coron. Artery Dis. Section Abstract Doc Link 8269196 Disease Relevance 0.54 Pain Relevance 0.10
VEGF-C secretion from TIVE (1800 pg/ml) and TIVE-LTC (2200 pg/ml) cells was comparable.


Localization (secretion) of LTC
4) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 0.52 Pain Relevance 0.04
Our studies report for the first time the role of KSHV induced MMP-2 and MMP-9 (Figure 8) secretion in HMVEC-d and latently infected TIVE-LTC cells.
Localization (secretion) of LTC associated with herpes simplex virus and metalloproteinase
5) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 1.42 Pain Relevance 0.56
Infected HMVEC-d and TIVE-LTC cells secreted a variety of ICs, GFs, angiogenic factors and matrix metalloproteinases (MMPs), which were significantly abrogated by COX-2 inhibition either by chemical inhibitors or by siRNA.
Localization (secreted) of LTC associated with metalloproteinase and cytokine
6) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Abstract Doc Link PMC2820536 Disease Relevance 1.72 Pain Relevance 0.37
TIVE-LTC cells secreted diminished levels of MMP-2 when compared to de novo infected cells (Figure 9E and 9G), therefore COX-2 inhibition could not effectively down-regulate active MMP-2 secretion during de novo infection (Figure 9E and 9F) compared to TIVE-LTC cells.
Localization (secreted) of LTC associated with metalloproteinase and infection
7) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 1.25 Pain Relevance 0.61
Similar to VEGF-A gene expression, TIVE-LTC cells secreted appreciably high levels of VEGF-A (54 pg/ml) as compared to TIVE cells and this secretion was effectively reduced upon treatment with COX inhibitors (Figure 6G).
Localization (secreted) of LTC
8) Confidence 0.01 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2820536 Disease Relevance 0.37 Pain Relevance 0.03

General Comments

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