ISSN: 2161-0460

Journal of Alzheimers Disease & Parkinsonism
Open Access

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Research Article

Protein Gelation around Axons Inhibits Action Potential Propagation in Nerve Fibers

Wade N Dauberman, Samuel Breit and Shaohua Xu*

Department of Biological Sciences, Florida Institute of Technology, 150 West University Blvd, Melbourne, FL 32901, USA

*Corresponding Author:
Shaohua Xu
Department of Biological Sciences
Florida Institute of Technology
150 West University Blvd, Melbourne
FL 32901
Tel: 321-674-8430
E-mail: shaohua@fit.edu

Received date: June 29, 2017; Accepted date: July 06, 2017; Published date: July 13, 2017

Citation: Dauberman WN, Breit S, Xu S (2017) Protein Gelation around Axons Inhibits Action Potential Propagation in Nerve Fibers. J Alzheimers Dis Parkinsonism 7:349. doi:10.4172/2161-0460.1000349

Copyright: © 2017 Dauberman WN, 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

Recently, we reported that amyloid fibers can further aggregate and form gels. In this paper, we provide evidence that protein gels, when formed outside nerve fibers, can substantially reduce the compound action potential. Protein gelation also increases the viscosity of the media. The nerve fiber’s compound action potential was found to be inversely related to the concentration of glycerol applied extracellularly. Soluble oligomer aggregates and fibrils on the other hand had little effect on action potential. These results suggest that the formation of protein gels surrounding neuronal processes, as in the case of amyloid plaques of Alzheimer’s disease, may disrupt the propagation of action potential and then trigger a cascade of events leading to neuronal death. As illustrated in Darcy’s law, gels restrict fluid flow and then the circulation of ions and molecules, which might underlie the pathogenesis of Alzheimer’s disease.

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