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ISSN: 2167-0277

Journal of Sleep Disorders & Therapy
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Editorial

Prion Proteins and Sleep Disturbances

Edward T Chang*, Camilo Fernandez-Salvador, Justin M Wei and Macario Camacho

Division of Otolaryngology, Tripler Army Medical Center, 1 Jarrett White Road, Tripler AMC, HI, USA

*Corresponding Author:
Edward T Chang
Division of Otolaryngology, Tripler Army Medical Center
1 Jarrett White Road, Tripler AMC, HI 96859, USA
Tel: 808-433-3181
E-mail: [email protected]

Received date: April 11, 2017; Accepted date: April 12, 2017; Published date: April 22, 2016

Citation: Chang ET, Salvador CF, Wei JM, Camacho M (2017) Prion Proteins and Sleep Disturbances. J Sleep Disord Ther 6: e139. doi: 10.4172/2167-0277.1000e139

Copyright: © 2017 Chang ET, 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

Prions normally exist as cellular membrane proteins. In humans, 209 amino acids with one disulfide bond form a primarily alpha-helical prion protein structure with a molecular mass of 35 to 36 kDa. The specific role and function of the prion protein elude research efforts and remains a controversial topic. Misfolding of the native prion protein leads to a protein structure with increased proportion of alpha-helices to beta-sheets. Advancing our understanding of the role of the prion protein as it relates to sleep and sleep disturbances presents an appealing avenue into diagnosing and more effectively treating a devastating and debilitating disease. New research into multiple system atrophy further validates evidence of a direct association between the prion protein and sleep. This reinforces previous observations regarding changes in sleep patterns noted with patients affected by Creutzfeldt-Jakob Disease and Fatal Familial Insomnia. From these earlier studies, a more focused approach to identifying and defining the role of the prion protein appears possible. A clearer understanding of the functional prion protein in its native role within the cell membrane allows identification of the potential signaling pathways and the aberration that likely occurs that leads to misfolding at the thermodynamic level. This discovery holds the greater, global potential of elucidating the mystery of proteopathies.

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