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2017 ; 37
(41
): 9808-9818
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Prying into the Prion Hypothesis for Parkinson s Disease
#MMPMID29021298
Brundin P
; Melki R
J Neurosci
2017[Oct]; 37
(41
): 9808-9818
PMID29021298
show ga
In Parkinson's disease, intracellular ?-synuclein inclusions form in neurons. We
suggest that prion-like behavior of ?-synuclein is a key component in Parkinson's
disease pathogenesis. Although multiple molecular changes are involved in the
triggering of the disease process, we propose that neuron-to-neuron transfer is a
crucial event that is essential for Lewy pathology to spread from one brain
region to another. In this review, we describe key findings in human postmortem
brains, cultured cells, and animal models of disease that support the idea that
?-synuclein can act as a prion. We consider potential triggers of the ?-synuclein
misfolding and why the aggregates escape cellular degradation under disease
conditions. We also discuss whether different strains of ?-synuclein fibrils can
underlie differences in cellular and regional distribution of aggregates in
different synucleinopathies. Our conclusion is that ?-synuclein probably acts as
a prion in human diseases, and a deeper understanding of this step in the
pathogenesis of Parkinson's disease can facilitate the development of
disease-modifying therapies in the future.Dual Perspectives Companion Paper:
Parkinson's Disease Is Not Simply a Prion Disorder, by D. James Surmeier, José A.
Obeso, and Glenda M. Halliday.
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