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International Journal of Cell Biology
Volume 2013 (2013), Article ID 141083, 6 pages
Review Article

Convergence of Synapses, Endosomes, and Prions in the Biology of Neurodegenerative Diseases

Department of Experimental Medical Science, Experimental Dementia Research Unit, Wallenberg Neuroscience Center, Lund University, 221 84 Lund, Sweden

Received 17 May 2013; Accepted 23 September 2013

Academic Editor: Alessio Cardinale

Copyright © 2013 Gunnar K. Gouras. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Age-related misfolding and aggregation of disease-linked proteins in selective brain regions is a characteristic of neurodegenerative diseases. Although neuropathological aggregates that characterize these various diseases are found at sites other than synapses, increasing evidence supports the idea that synapses are where the pathogenesis begins. Understanding these diseases is hampered by our lack of knowledge of what the normal functions of these proteins are and how they are affected by aging. Evidence has supported the idea that neurodegenerative disease-linked proteins have a common propensity for prion protein-like cell-to-cell propagation. However, it is not thought that the prion-like quality of these proteins/peptides that allows their cell-to-cell transmission implies a role for human-to-human spread in common age-related neurodegenerative diseases. It will be important to better understand the molecular and cellular mechanisms governing the role of these aggregating proteins in neural function, especially at synapses, how their propagation occurs and how pathogenesis is promoted by aging.