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2013 ; 1
(1
): 79
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Molecular chaperones and protein folding as therapeutic targets in Parkinson s
disease and other synucleinopathies
#MMPMID24314025
Ebrahimi-Fakhari D
; Saidi LJ
; Wahlster L
Acta Neuropathol Commun
2013[Dec]; 1
(1
): 79
PMID24314025
show ga
Changes in protein metabolism are key to disease onset and progression in many
neurodegenerative diseases. As a prime example, in Parkinson's disease, folding,
post-translational modification and recycling of the synaptic protein ?-synuclein
are clearly altered, leading to a progressive accumulation of pathogenic protein
species and the formation of intracellular inclusion bodies. Altered protein
folding is one of the first steps of an increasingly understood cascade in which
?-synuclein forms complex oligomers and finally distinct protein aggregates,
termed Lewy bodies and Lewy neurites. In neurons, an elaborated network of
chaperone and co-chaperone proteins is instrumental in mediating protein folding
and re-folding. In addition to their direct influence on client proteins,
chaperones interact with protein degradation pathways such as the
ubiquitin-proteasome-system or autophagy in order to ensure the effective removal
of irreversibly misfolded and potentially pathogenic proteins. Because of the
vital role of proper protein folding for protein homeostasis, a growing number of
studies have evaluated the contribution of chaperone proteins to
neurodegeneration. We herein review our current understanding of the involvement
of chaperones, co-chaperones and chaperone-mediated autophagy in
synucleinopathies with a focus on the Hsp90 and Hsp70 chaperone system. We
discuss genetic and pathological studies in Parkinson's disease as well as
experimental studies in models of synucleinopathies that explore molecular
chaperones and protein degradation pathways as a novel therapeutic target. To
this end, we examine the capacity of chaperones to prevent or modulate
neurodegeneration and summarize the current progress in models of Parkinson's
disease and related neurodegenerative disorders.
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