Open AccessPyridoxine Decreases Oxidative Stress on Human Erythrocyte Membrane Protein in vitro
Author(s) -
Margarita María Velásquez,
Darío Méndez,
Carlos Moneriz
Publication year - 2019
Publication title -
the open biochemistry journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.325
H-Index - 13
ISSN - 1874-091X
DOI - 10.2174/1874091x01913010037
Subject(s) - pyridoxine , oxidative stress , cumene hydroperoxide , lipid peroxidation , chemistry , protein carbonylation , biochemistry , malondialdehyde , oxidative phosphorylation , catalysis
Background: Pyridoxine has reduction and prevention against the levels of reactive oxygen species in in vitro studies. However, the biochemical mechanism that explains this behavior has not yet been fully clarified. Objective: To evaluate the effect of pyridoxine against oxidative damage on the membrane of human erythrocytes. Methods: Cumene hydroperoxide was used to induce oxidative stress in protein and lipid. Human erythrocytes were incubated with pyridoxine and cumene hydroperoxide, either alone or together for 8 h. Oxidative damage was determined by measuring lipid peroxidation and membrane protein carbonylation. Results: The results indicate that the malondialdehyde concentration decreased with increasing concentration of pyridoxine. The membrane protein content also decreased with increasing concentration of vitamin B6, which was confirmed by the decreased signal intensity in the western blot when compared to control without pyridoxine. Results demonstrate that pyridoxine can significantly decrease lipid peroxidation and protein carbonylation in red cell membrane exposed to high concentrations of oxidant agent. Conclusion: Pyridoxine showed a protective effect against the oxidative stress in human erythrocytes in vitro , inhibiting the carbonylation and the oxidative damage of erythrocyte membrane proteins. To date, such an effect has not yet been reported in terms of protein oxidation.