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Last Updated: 3 months ago

Possible Interaction: Dinitrochlorobenzene and Glutathione

Research Papers that Mention the Interaction

DNCB reduced GSH levels and up‐regulated bcl‐2 gene expression unlike CinA.Chemical reactivity controls Nrf2‐dependent genes having protective effect in DC.
Unlike CinA, DNCB treatment provoked a significant reduction of intracellular GSH levels and up‐regulated bcl‐2 gene expression, under the control of Nrf2.
Toxicology and applied pharmacology  •  2017  |  View Paper
This hypothesis was tested by asking two questions: (1) do glutathione-supplemented … augmented lung protection compared with control platelets, and (2) does conjugation of platelet glutathione … 1-chloro-2,4-dinitrobenzene or inactivation of catalase with 3-amino-1,2,…-triazole decrease in vitro platelet metabolism of hydrogen peroxide?
Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis  •  1992  |  View Paper
The sensing signal was based on the inhibition of the colorimetric reaction between 1-chloro-dinitrobenzene (CDNB) and GSH , catalyzed by the sol-gel entrapped enzyme.
Current pharmaceutical biotechnology  •  2018  |  View Paper
After each exposure to DNCB , the level of GSH is diminished in a dose dependent manner.
Toxicological sciences : an official journal of the Society of Toxicology  •  2016  |  View Paper
We found that 2,4-dinitrohalobenzenes deplete the GSH present in HaCaT cells within the first hour of exposure, in a dose dependent manner.
Toxicology letters  •  2015  |  View Paper
Surprisingly, treatment … doses of 1-chloro-2,4-dinitrobenzene (CDNB; 5 µM) or … mM), which transiently deplete GSH levels to about 40% of control levels, resulted in enhanced differentiation of HL-60 cells exposed …-trans-retinoic acid (ATRA), as well as under un-induced conditions (i.e., spontaneous differentiation).
Oxidative medicine and cellular longevity  •  2010  |  View Paper
Dinitrochlorobenzene treatment , which inhibited cellular thioredoxin reductase and partially depleted GSH , caused reversible oxidation of several proteins, including thioredoxin 1 and peroxiredoxins 1 and 2.
The Biochemical journal  •  2005  |  View Paper
Glutathione conjugation of CDNB metabolism was 10-fold higher in M1 than in M2, but was still much lower than in human hepatocytes.
Xenobiotica; the fate of foreign compounds in biological systems  •  2004  |  View Paper
In the renal cortex and in lung the rate of glutathione conjugation with CDNB was a little but significantly (p < 0.05) higher in women than men, whereas no sex-dependent difference was observed in the liver and colon.
International journal of clinical pharmacology and therapeutics  •  1995  |  View Paper
The results show a CDNB dose-dependent reduction in GSH content, the magnitude of intracellular free calcium mobilization, and the extent of tyrosine phosphorylation of several proteins, including phospholipase C-gamma 1.
Toxicology and applied pharmacology  •  1993  |  View Paper
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