alexa Cotinine Inhibits Amyloid-β Peptide Neurotoxicity and Oligomerization
ISSN: 2161-0495

Journal of Clinical Toxicology
Open Access

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Research Article

Cotinine Inhibits Amyloid-β Peptide Neurotoxicity and Oligomerization

Sarah Burgess1, Ross Zeitlin1,2 and Valentina Echeverria1,2,3*

1Research Chemist, Research and Development, Department of Veterans Affairs, Bay Pines VA Healthcare System, Bay Pines, FL, USA

2Tampa VA Healthcare System, Tampa, FL, USA

3Department of Molecular Medicine, University of South Florida, Tampa, FL 33647, USA

*Corresponding Author:
Valentina Echeverria, Ph.D
10,000 Bay Pines Blvd., Bldg. 23, Rm. 123
Bay Pines, FL 33744, USA
Tel: +727-398-6661 (Ext. 4425)
Fax: +727-319-1161
E-mail: [email protected]

Received date: March 21, 2012; Accepted date: April 17, 2012; Published date: April 20, 2012

Citation: Burgess S, Zeitlin R, Echeverria V (2012) Cotinine Inhibits Amyloid-ß Peptide Neurotoxicity and Oligomerization. J Clinic Toxicol S6:003. doi: 10.4172/2161-0495.S6-003

Copyright: © 2012 Burgess S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Alzheimer’s disease, the main cause of dementia, correlates with an increase in the brain levels of aggregated forms of amyloid-β (Aβ) peptide. We investigated the effect of cotinine, the main metabolite of nicotine, on Aβ 1-42 neurotoxicity. Compared to nicotine, cotinine has a longer plasma half-life, lower toxicity and is a poor agonist of the nicotinic acetylcholine receptors (nAChRs). We found that cotinine promoted the survival of primary cortical neurons exposed to Aβ 1-42 . This neuroprotective effect was independent of the agonistic activation of the nAChRs and it was not prevented by the general nAChR antagonist mecamylamine. However, it was prevented by the pre-aggregation of Aβ in absence of cotinine, suggesting that inhibition of Aβ 1-42 aggregation by cotinine is a key mechanism mediating its neuroprotective activity. The analysis of Aβ 1-42 aggregation using dot blot immunoassay showed that cotinine inhibits its oligomerization. These results suggest that cotinine is neuroprotective at least in part by preventing the aggregation of the amyloid peptide. We previously found that cotinine prevented memory loss and reduced plaques in the brain of Tg6799 mice. This study suggests that cotinine can also inhibit neuronal cell death induced by Aβ neurotoxicity.

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