title: [Role of glycolysis and antioxidant enzymes in the toxicity of amyloid beta peptide Abeta25-35 to erythrocytes].
abstract: 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) .
authors.forename: E A
authors.initials: EA
authors.lastname: Kosenko
authors.forename: I N
authors.initials: IN
authors.lastname: Solomadin
authors.forename: N V
authors.initials: NV
authors.lastname: Marov
authors.forename: N I
authors.initials: NI
authors.lastname: Venediktova
authors.forename: A S
authors.initials: AS
authors.lastname: Pogosian
authors.forename: Iu G
authors.initials: IuG
authors.lastname: Kaminskiĭ
mesh_terms: D016229:Amyloid beta-Peptides / Q000502:physiology / Q000633:toxicity*; D000818:Animals; D000975:Antioxidants / Q000378:metabolism*; D002374:Catalase / Q000037:antagonists & inhibitors; D003470:Culture Media; D004912:Erythrocytes / Q000166:cytology / Q000187:drug effects* / Q000201:enzymology; D037741:Fullerenes / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000037:antagonists & inhibitors; D006019:Glycolysis; D006801:Humans; D066298:In Vitro Techniques; D010042:Ouabain / Q000494:pharmacology; D010446:Peptide Fragments / Q000502:physiology / Q000633:toxicity*; D011190:Potassium Cyanide / Q000494:pharmacology; D051381:Rats; D019810:Sodium Azide / Q000494:pharmacology; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors; D013045:Species Specificity; D013482:Superoxide Dismutase / Q000037:antagonists & inhibitors; D013870:Thiomalates / Q000494:pharmacology; D055815:Young Adult
chemical_list: D016229:Amyloid beta-Peptides; D000975:Antioxidants; D003470:Culture Media; D037741:Fullerenes; D010446:Peptide Fragments; D013870:Thiomalates; C074636:amyloid beta-protein (25-35); D010042:Ouabain; C046062:2-thiomalic acid; D019810:Sodium Azide; D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D000254:Sodium-Potassium-Exchanging ATPase; D005947:Glucose; D011190:Potassium Cyanide; C069837:fullerene C60