| 19060940 |
Kosenko EA, Solomadin IN, Marov NV, Venediktova NI, Pogosian AS, Kaminskii IuG: [Role of glycolysis and antioxidant enzymes in the toxicity of amyloid beta peptide Abeta25-35 to erythrocytes]. Bioorg Khim. 2008 Sep-Oct;34(5):654-60.
The role of glycolysis and antioxidant enzymes in amyloid beta peptide Abeta (25-35) toxicity to human and rat erythrocytes was studied. The erythrotoxicity of Abeta (25-35) was shown to increase two- to fourfold both in the absence of glucose in the incubation medium and upon the addition of sodium fluoride, an enolase inhibitor. Potassium cyanide, a Cu,Zn-superoxide dismutase inhibitor, abolishes the toxic effect of Abeta (25-35) to erythrocytes, whereas mercaptosuccinate, a glutathione peroxidase inhibitor, and ouabain, a Na+,K+-ATPase inhibitor, promote it. Sodium azide, a catalase inhibitor, did not affect the cell lysis under the action of Abeta (25-35) . The results support the hypothesis that H2O2, Cu,Zn superoxide dismutase, and glutathione peroxidase are involved in the toxicity mechanism rather than superoxide radical. Glycolysis and Na+,K+-ATPase play a substantial protective role. Fullerene C (60) nanoparticles are toxic to erythrocytes of both types; their toxicity is not related to enhanced oxidative stress and the mechanism of toxicity differs from that of Abeta (25-35) . |
31(0,1,1,1) |