Hydrogen peroxide-induced glutathione depletion and aldehyde dehydrogenase inhibition in erythrocytes
References (29)
- et al.
Toxic. appl. Pharmac.
(1981) - et al.
Toxic. Lett.
(1982) Archs Biochem. Biophys.
(1959)- et al.
- et al.
- et al.
Analyt. Biochem.
(1984) J. Free Radicals Biol. Med.
(1985)- et al.
- et al.
J. biol. Chem.
(1970) - et al.
J. Pharmac. exp. Ther.
(1981)
Br. J. Haemat.
Alcoholism Clin. expl Res.
J. Pharmac. exp. Ther.
J. Lab. clin. Med.
Cited by (12)
Protective effects of ferulic acid and related polyphenols against glyoxal- or methylglyoxal-induced cytotoxicity and oxidative stress in isolated rat hepatocytes
2015, Chemico-Biological InteractionsCitation Excerpt :The increased hepatotoxicity was mainly due to the enhanced conversion of fructose and fructose metabolites to form GO which could produce reactive radicals leading to increased ROS formation [1]. Increased H2O2 cellular concentrations may also impair ALDH2 by oxidizing a cysteine residue (C302) at the binding pocket and increase GO levels thereby increasing cytotoxicity [3,17]. Polyphenols have been studied extensively for their therapeutic benefits.
The effects of nitroxyl (HNO) on H<inf>2</inf>O<inf>2</inf> metabolism and possible mechanisms of HNO signaling
2013, Archives of Biochemistry and BiophysicsCitation Excerpt :Thus, at the high concentrations of HNO used in our studies, it is very possible that GSH levels can be depleted leading to a decrease in H2O2 handling. Significantly, H2O2 is also known to deplete GSH levels in cells (for example, [52]), further illustrating the similarity between H2O2 and HNO biological activity. The results discussed herein support the idea of a possible strong and close relationship between the chemical biology of H2O2 and HNO.
Differences in glyoxal and methylglyoxal metabolism determine cellular susceptibility to protein carbonylation and cytotoxicity
2011, Chemico-Biological InteractionsCitation Excerpt :Other aldehydes, such as acetaldehyde, formaldehyde, propionaldehyde, and chloroacetaldehyde, which are all ALDH2 substrates, also significantly increased hepatocyte cytotoxicity in the inflammatory hepatocyte model [39]. It is proposed that H2O2 inhibits ALDH2 by oxidizing the cysteine residue (C302) at the binding pocket of ALDH2 [38,39]. ALDH2 also plays a critical role in detoxifying GO.
Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity
2011, Chemico-Biological InteractionsCitation Excerpt :Moreover, recombinant ALDH7A1 was unable to metabolize 4HNE without prior activation with the reducing agent. Oxidants such as H2O2 are known to significantly inhibit erythrocyte aldehyde dehydrogenase I activity [53]. This implies that as oxidative stress increases within the cell the activity and substrate specificity of ALDH7A1 may be significantly altered.
Protection by a radical scavenger edaravone against cisplatin-induced nephrotoxicity in rats
2002, European Journal of PharmacologyReversible oxidation of glyceraldehyde 3-phosphate dehydrogenase thiols in human lung carcinoma cells by hydrogen peroxide
1987, Biochemical and Biophysical Research Communications