Two novel polysaccharides from the torus of Saussurea laniceps protect against AAPH-induced oxidative damage in human erythrocytes

2018 ◽  
Vol 200 ◽  
pp. 446-455 ◽  
Author(s):  
Wenbo Chen ◽  
Juanjuan Ma ◽  
Fan Gong ◽  
Hongru Xi ◽  
Qiping Zhan ◽  
...  
2016 ◽  
Vol 40 (12) ◽  
pp. 1320-1331 ◽  
Author(s):  
Fariheen Aisha Ansari ◽  
Shaikh Nisar Ali ◽  
Riaz Mahmood

Biochemistry ◽  
1997 ◽  
Vol 36 (22) ◽  
pp. 6768-6776 ◽  
Author(s):  
Kitty de Jong ◽  
Danielle Geldwerth ◽  
Frans A. Kuypers

2007 ◽  
Vol 45 (1) ◽  
pp. 130-135 ◽  
Author(s):  
M. Suwalsky ◽  
P. Orellana ◽  
M. Avello ◽  
F. Villena

2019 ◽  
Vol 13 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Margarita Velásquez ◽  
Darío Méndez ◽  
Carlos Moneriz

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.


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