INT158340

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Context Info
Confidence 0.58
First Reported 2009
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 13
Total Number 15
Disease Relevance 2.76
Pain Relevance 1.64

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

mitochondrion (ALDH2) small molecule metabolic process (ALDH2) oxidoreductase activity (ALDH2)
carbohydrate metabolic process (ALDH2)
Anatomy Link Frequency
blood 1
blood vessels 1
ALDH2 (Homo sapiens)
Pain Link Frequency Relevance Heat
tolerance 24 98.48 Very High Very High Very High
alcohol 315 97.32 Very High Very High Very High
Glutamate 19 84.16 Quite High
Potency 16 80.36 Quite High
headache 7 71.56 Quite High
Bioavailability 32 31.44 Quite Low
Angina 11 5.00 Very Low Very Low Very Low
depression 9 5.00 Very Low Very Low Very Low
ischemia 8 5.00 Very Low Very Low Very Low
addiction 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Alcohol Addiction 80 99.92 Very High Very High Very High
Increased Venous Pressure Under Development 35 95.28 Very High Very High Very High
Targeted Disruption 8 77.52 Quite High
Headache 7 71.56 Quite High
Dizziness 4 71.00 Quite High
Vomiting 7 70.56 Quite High
Disease 39 58.56 Quite High
Alcoholic Cardiomyopathy 6 35.20 Quite Low
Cv Unclassified Under Development 33 30.32 Quite Low
Cancer 45 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Two of the three siRNAs were active, yielding a 65-75% reduction of ALDH2 activity.
Negative_regulation (reduction) of ALDH2
1) Confidence 0.58 Published 2009 Journal Alcohol Section Abstract Doc Link 19251111 Disease Relevance 0.44 Pain Relevance 0.29
This effect is consistent with a 50% reduction in ALDH2 mRNA, whereas neither beta-actin mRNA nor the interferon-inducible transmembrane protein-1 mRNA levels were affected.
Negative_regulation (reduction) of ALDH2 mRNA
2) Confidence 0.58 Published 2009 Journal Alcohol Section Abstract Doc Link 19251111 Disease Relevance 0.35 Pain Relevance 0.26
After transfection of HEK-293 cells, one of the genes was shown to be active, yielding a 50% reduction of ALDH2 activity.
Negative_regulation (reduction) of ALDH2
3) Confidence 0.58 Published 2009 Journal Alcohol Section Abstract Doc Link 19251111 Disease Relevance 0.37 Pain Relevance 0.26
This study describes chemically synthesized siRNAs and an endogenously synthesized shRNA, which reduce ALDH2 activity and constitute tools that should be of value for further alcohol research.
Negative_regulation (reduce) of ALDH2 associated with alcohol
4) Confidence 0.43 Published 2009 Journal Alcohol Section Abstract Doc Link 19251111 Disease Relevance 0.11 Pain Relevance 0.17
In addition, findings from Kawamoto’s group indicated that deficiency in ALDH2 enzymatic activity inhibits acetate formation via acetaldehyde [123].
Negative_regulation (deficiency) of ALDH2
5) Confidence 0.43 Published 2010 Journal International Journal of Environmental Research and Public Health Section Body Doc Link PMC2872347 Disease Relevance 0.47 Pain Relevance 0.18
Prevalence of the ALDH2*1 allele is associated with alcoholism.
Negative_regulation (Prevalence) of ALDH2 associated with alcohol addiction
6) Confidence 0.42 Published 2010 Journal International Journal of Environmental Research and Public Health Section Body Doc Link PMC2872347 Disease Relevance 0.47 Pain Relevance 0.18
Both Equations 3 and 4 predict that ALDH2 inactivation should result in first order decay of the NO signal with the observed rate constant corresponding to (0.5–1.0) × kinact.



Negative_regulation (inactivation) of ALDH2
7) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0
If inactivation of vascular ALDH2 were indeed a major cause of nitrate tolerance, these results would imply delayed tolerance development in subjects carrying the mutation.
Negative_regulation (inactivation) of ALDH2 associated with tolerance
8) Confidence 0.41 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0.10
Similarly, inactivation of ALDH2 in nitrate-tolerant blood vessels results in the loss of 1,2-GDN selectivity (10, 37, 38).
Negative_regulation (inactivation) of ALDH2 in blood vessels
9) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0
Inhibition of ALDH2 by high NAD has been observed previously (28, 39) and was suggested to result from competition for p-NPA binding (28).
Negative_regulation (Inhibition) of ALDH2
10) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0
As shown in Fig. 4B, the esterase activities of ALDH2*1 and ALDH2*2 were maximally stimulated by 1 and 5 mm NAD, respectively, whereas higher concentrations of the coenzyme led to marked inhibition of both ALDH2 variants.
Negative_regulation (inhibition) of ALDH2
11) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0
At low micromolar GTN concentrations the ALDH2-catalyzed reaction results in highly selective formation of 1,2-GDN, but this selectivity is lost at high substrate concentrations or in the presence of ALDH2 inhibitors (9, 10).
Negative_regulation (inhibitors) of ALDH2
12) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0.08 Pain Relevance 0
The present results indicate that Alda-1 stimulates established ALDH2 activities by improving NAD binding but does not improve the GTN binding affinity of the Asian variant.
Negative_regulation (established) of ALDH2
13) Confidence 0.40 Published 2010 Journal The Journal of Biological Chemistry Section Abstract Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0.04
Deficiency in ALDH2 due to point mutation in the active ALDH2*1 gene, significantly alters blood acetaldehyde levels and vulnerability for alcoholism [124].
Negative_regulation (Deficiency) of ALDH2 in blood associated with alcohol addiction
14) Confidence 0.37 Published 2010 Journal International Journal of Environmental Research and Public Health Section Body Doc Link PMC2872347 Disease Relevance 0.47 Pain Relevance 0.18
20-fold left shift of NAD-induced inhibition of wild type ALDH2, which was half-maximal at ?
Negative_regulation (inhibition) of ALDH2
15) Confidence 0.35 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2801295 Disease Relevance 0 Pain Relevance 0

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