MovDisordV3, Main, Merge, bibRecord, 000000

Alpha-synuclein propagation: New insights from animal models.

Identifieur interne : 000000 ( Main/Merge ); suivant : 000001

Alpha-synuclein propagation: New insights from animal models.

Auteurs : Benjamin Dehay [France] ; Miquel Vila [Espagne] ; Erwan Bezard [France] ; Patrik Brundin [Suède] ; Jeffrey H. Kordower [États-Unis]

Source :

Movement Disorders [ 0885-3185 ] ; 2015-09-08.

RBID : Hal:hal-01205919

Abstract

Aggregation of alpha-synuclein is implicated in several neurodegenerative diseases collectively termed synucleinopathies. Emerging evidence strongly implicates cell-to-cell transmission of misfolded alpha-synuclein as a common pathogenetic mechanism in synucleinopathies. The impact of alpha-synuclein pathology on neuronal dysfunction and behavioral impairments is being explored in animal models. This review provides an update on how research in animal models supports the concept that misfolded alpha-synuclein spreads from cell to cell and describes how findings in animal models might relate to the disease process in humans. Finally, we discuss the current underlying molecular and cellular mechanisms and future therapeutic strategies targeting alpha-synuclein propagation. © 2015 International Parkinson and Movement Disorder Society.

Url:

DOI: 10.1002

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Hal:hal-01205919

Le document en format XML

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<front><div type="abstract" xml:lang="en">Aggregation of alpha-synuclein is implicated in several neurodegenerative diseases collectively termed synucleinopathies. Emerging evidence strongly implicates cell-to-cell transmission of misfolded alpha-synuclein as a common pathogenetic mechanism in synucleinopathies. The impact of alpha-synuclein pathology on neuronal dysfunction and behavioral impairments is being explored in animal models. This review provides an update on how research in animal models supports the concept that misfolded alpha-synuclein spreads from cell to cell and describes how findings in animal models might relate to the disease process in humans. Finally, we discuss the current underlying molecular and cellular mechanisms and future therapeutic strategies targeting alpha-synuclein propagation. © 2015 International Parkinson and Movement Disorder Society.</div>
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<front><div type="abstract" xml:lang="en">Aggregation of alpha-synuclein is implicated in several neurodegenerative diseases collectively termed synucleinopathies. Emerging evidence strongly implicates cell-to-cell transmission of misfolded alpha-synuclein as a common pathogenetic mechanism in synucleinopathies. The impact of alpha-synuclein pathology on neuronal dysfunction and behavioral impairments is being explored in animal models. This review provides an update on how research in animal models supports the concept that misfolded alpha-synuclein spreads from cell to cell and describes how findings in animal models might relate to the disease process in humans. Finally, we discuss the current underlying molecular and cellular mechanisms and future therapeutic strategies targeting alpha-synuclein propagation. © 2015 International Parkinson and Movement Disorder Society.</div>
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<country>France</country>
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<orgName type="university">Université de Bordeaux</orgName>
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<author><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name>
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<country>France</country>
<placeName><settlement type="city">Bordeaux</settlement>
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<orgName type="university">Université de Bordeaux</orgName>
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<date when="2012-02-29">2012-02-29</date>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Toward an animal model of restless legs syndrome?</title>
<author><name sortKey="Ghorayeb, Imad" sort="Ghorayeb, Imad" uniqKey="Ghorayeb I" first="Imad" last="Ghorayeb">Imad Ghorayeb</name>
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<orgName type="acronym">IMN</orgName>
<desc><address><addrLine>Bât. 3b 1er étage 146 Rue Léo Saignat 33076 Bordeaux </addrLine>
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<desc><address><addrLine>35, place Pey Berland - 33076 Bordeaux</addrLine>
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</address>
<ref type="url">http://www.u-bordeaux.fr/</ref>
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<country>France</country>
<placeName><settlement type="city">Bordeaux</settlement>
<region type="region" nuts="2">Aquitaine</region>
</placeName>
<orgName type="university">Université de Bordeaux</orgName>
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<author><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name>
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<idno type="DOI">10.1002</idno>
<series><title level="j">Movement Disorders</title>
<idno type="ISSN">0885-3185</idno>
<imprint><date type="datePub">2012-02-29</date>
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<front><div type="abstract" xml:lang="en">Parkinson disease (PD) is a progressive neurodegenerative disorder pathologically characterized by the loss of dopaminergic neurons from the substantia nigra pars compacta and the presence, in affected brain regions, of protein inclusions named Lewy bodies (LBs). The ATP13A2 gene (locus PARK9) encodes the protein ATP13A2, a lysosomal type 5 P-type ATPase that is linked to autosomal recessive familial parkinsonism. The physiological function of ATP13A2, and hence its role in PD, remains to be elucidated. Here, we show that PD-linked mutations in ATP13A2 lead to several lysosomal alterations in ATP13A2 PD patient-derived fibroblasts, including impaired lysosomal acidification, decreased proteolytic processing of lysosomal enzymes, reduced degradation of lysosomal substrates, and diminished lysosomal-mediated clearance of autophagosomes. Similar alterations are observed in stable ATP13A2-knockdown dopaminergic cell lines, which are associated with cell death. Restoration of ATP13A2 levels in ATP13A2-mutant/depleted cells restores lysosomal function and attenuates cell death. Relevant to PD, ATP13A2 levels are decreased in dopaminergic nigral neurons from patients with PD, in which ATP13A2 mostly accumulates within Lewy bodies. Our results unravel an instrumental role of ATP13A2 deficiency on lysosomal function and cell viability and demonstrate the feasibility and therapeutic potential of modulating ATP13A2 levels in the context of PD.</div>
</front>
</TEI>
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Movement Disorders (revue)

Alpha-synuclein propagation: New insights from animal models.

Alpha-synuclein propagation: New insights from animal models.

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