Milton, Nathaniel G.N. (2001) Inhibition of catalase activity with 3-amino-triazole enhances the cytotoxicity of the Alzheimer’s amyloid-ß peptide. NeuroToxicology, 72 (6). pp. 767-774. ISSN 0161-813XFull text not available from this repository.
Amyloid-? (A?) is a cytotoxic peptide implicated in the pathology of Alzheimer’s disease. The antioxidant enzyme catalase has been suggested to protect against A? cytotoxicity in both neuronal and non-neuronal cell types. Inhibition of endogenous catalase using 3-amino-1,2,4-triazole (3AT) in neuronal (NT-2) and myeloma (SP2/0-Ag-14) cell lines increases A? toxicity, suggesting that any protective role for endogenous catalase requires active enzyme. In A? treated myeloma cells there was a significant decrease in the total cell catalase activity and immunoreactivity. However, when the surviving live cell population was isolated following A? treatment the levels of catalase were significantly increased. The surviving live cell population from groups treated with both 3AT and A? contain elevated immunoreactive catalase levels suggesting that the protective role for endogenous catalase may have a component independent of the antioxidant activity, possibly by acting as an A? binding protein. Amyloid-? (A?) cytotoxicity can be prevented by Vitamin E treatment or an anti-A? monoclonal antibody (ALI01), both of which also prevent A? cytotoxicity in cells treated with 3AT. These observations suggest that A? mediated cell death in both neuronal and non-neuronal cells is mediated in part by actions to increase hydrogen peroxide. Catalase has a protective role, as a hydrogen peroxide-degrading enzyme and catalase inhibition by A? is not the direct cause of cytotoxicity.
|Subjects:||University of Westminster > Science and Technology > Life Sciences, School of (No longer in use)|
|Depositing User:||Miss Nina Watts|
|Date Deposited:||26 Jan 2010 15:42|
|Last Modified:||26 Jan 2010 15:42|
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