alexa Anatabine Attenuates Tau Phosphorylation and Oligomerization in P301S Tau Transgenic Mice
ISSN: 2168-975X

Brain Disorders & Therapy
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Research Article

Anatabine Attenuates Tau Phosphorylation and Oligomerization in P301S Tau Transgenic Mice

Daniel Paris1*, David Beaulieu-Abdelahad1, Ghania Ait-Ghezala1, Venkat Mathura1, Megha Verma1, Alex E Roher3, Jon Reed1,Fiona Crawford1 and Michael Mullan1,2
1Roskamp Institute, Sarasota, Florida, USA
2Rock Creek Pharmaceuticals, Gloucester, Massachusetts, USA
3The Longtine Center for Neurodegenerative Biochemistry, Banner Sun Health Research Institute, Sun City, Arizona, USA
Corresponding Author : Daniel Paris
Roskamp Institute, Sarasota, Florida, USA
Tel: 941-752-2949
Fax: 941-752-2948
E-mail: [email protected]
Received April 21, 2014; Accepted May 21, 2014; Published May 21, 2014
Citation: Paris D, Beaulieu-Abdelahad D, Ait-Ghezala G, Mathura V, Verma M, et al, (2014) Anatabine Attenuates Tau Phosphorylation and Oligomerization in P301S Tau Transgenic Mice. Brain Disord Ther 3:126. doi:10.4172/2168-975X.1000126
Copyright: © 2013 Paris D, 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

We have previously shown that the natural alkaloid anatabine displays some anti-inflammatory and Alzheimer amyloid (Aβ) lowering properties in the central nervous system associated with reduced STAT3 and NFkB activation. We investigated here the impact of a chronic oral treatment with anatabine in a model of tauopathy. We found that anatabine reduces the incidence of paralysis and abnormal hind limb extension reflex while improving rotarod performances in P301S mutant human Tau transgenic mice (Tg Tau P301S) suggesting that anatabine delays the disease progression in this model of tauopathy. Analyzes of brain and spinal cord homogenates reveal that anatabine reduces tau phosphorylation at multiple pertinent Alzheimer’s disease (AD) epitopes and decreases the levels of pathological tau conformers/oligomers in both detergent soluble and insoluble fractions. Pathological tau species reduction induced by anatabine was accompanied by decreased Iba1 expression suggesting a diminution of microgliosis in the brain and spinal cord of Tg Tau P301S mice. In addition, we found that anatabine administration increases phosphorylation of the inhibitory residue (Ser9) of glycogen synthase kinase-3β, a primary tau kinase, associated with AD pathology, providing a possible mechanism for the observed reduction of tau phosphorylation. These data support further exploration of anatabine as a possible disease modifying agent for neurodegenerative tauopathies and, in particular AD, since anatabine also displays Aβ lowering properties.

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