Role of glycolysis and antioxidant enzymes in the toxicity of amyloid beta peptide Aβ25–35 to erythrocytes

摘要

The role of glycolysis and antioxidant enzymes in amyloid beta peptide Aβ25–35 toxicity to human and rat erythrocytes was studied. The erythrotoxicity of Aβ25–35 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 Aβ25–35 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 Aβ25–35. 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 C60 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 Aβ25–35.