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Last Updated: 2 years ago

Possible Interaction: Glutathione and Hydrogen Peroxide

Research Papers that Mention the Interaction

The deleterious effects of either H2O2 or IL-1β could be efficiently prevented by glutathione.
Connective tissue research  •  2014  |  View Paper
They catalyze the reduction of hydrogen peroxide or organic hydroperoxides using glutathione.
Biochemical pharmacology  •  2020  |  View Paper
The Cu2+ in the CuS:Gd NPs could be reduced to Cu+ by GSH in tumors, which further reacted with H2O2 and triggered Fenton-like reaction to simultaneously generate abundant ·OH and deplete GSH for tumor enhanced CDT.
Journal of Nanobiotechnology  •  2019  |  View Paper
To examine whether the protein-bound DA conjugates exhibit pro-oxidant activities, we measured the depletion of glutathione (GSH) with the concomitant production of hydrogen peroxide.
International journal of molecular sciences  •  2019  |  View Paper
Application of up to 100 µM hydrogen peroxide did not affect the cell viability for up to 4h, but caused a time- and concentration-dependent increase in the extracellular glutathione ( GSH ) content that was accompanied by a matching decrease in the cellular GSH content.
Hydrogen peroxide at 100 µM stimulated maximally the GSH export from viable neurons, but did not affect GSH export from cultured astrocytes.
Free radical biology & medicine  •  2014  |  View Paper
The effect was not seen at 1 mM H2O2 and was counteracted by glutathione.
Platelets  •  2013  |  View Paper
Experiments on skinned fibres show that these effects can be attributed to H2O2 interacting with glutathione and myoglobin, respectively.
The Journal of physiology  •  2011  |  View Paper
In whole-cell recordings and inside-out patches, H2O2 or diamide caused a strong inhibition of the vascular KATP channel (Kir6.1/SUR2B) in the presence, but not in the absence, of glutathione (GSH).
The Journal of Biological Chemistry  •  2010  |  View Paper
Furthermore the cytotoxicity and proteasome inhibition induced by DA, AM and H2O2 could be abrogated by GSH , ascorbic acid (AA), Vitamin E, SOD (superoxidase dismutase) or CAT (catalase) with different profiles.
Free radical research  •  2009  |  View Paper
In the present studies, we found that direct exposure of purified 26 S proteasomes to H2O2 had negligible effects on their activity, whereas incubation with glutathione and H2O2 produced >80% decrease in chymotrypsin-like and trypsin-like activities.
The Journal of Biological Chemistry  •  2009  |  View Paper
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