Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration
Identifieur interne : 000F05 ( Ncbi/Checkpoint ); précédent : 000F04; suivant : 000F06Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration
Auteurs : Benjamin Dehay [France] ; Alfredo Ramirez [Allemagne] ; Marta Martinez-Vicente [Espagne] ; Celine Perier [Espagne] ; Marie-Hélène Canron [France] ; Evelyne Doudnikoff [France] ; Anne Vital [France] ; Miquel Vila [Espagne] ; Christine Klein [Allemagne] ; Erwan Bezard [France]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2012.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Adenosine Triphosphatases.
- enzymology : Parkinson Disease.
- metabolism : Lysosomes, Parkinson Disease.
- pathology : Parkinson Disease.
- Cell Line, Gene Knockdown Techniques, Humans.
Abstract
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
Url:
DOI: 10.1073/pnas.1112368109
PubMed: 22647602
PubMed Central: 3386132
Affiliations:
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PMC:3386132Le document en format XML
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<author><name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">Neurodegenerative Diseases Research Group, Vall d’Hebron Research Institute,<institution>Centro Investigación Biomédica en Red Enfermedades Neurodegenerativas</institution>
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<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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, 08193 Bellaterra, Barcelona,<country>Spain</country>
</nlm:aff>
<country xml:lang="fr">Espagne</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Klein, Christine" sort="Klein, Christine" uniqKey="Klein C" first="Christine" last="Klein">Christine Klein</name>
<affiliation wicri:level="1"><nlm:aff id="aff2">Section of Clinical and Molecular Neurogenetics, Department of Neurology,<institution>University of Lubeck</institution>
, 23538 Lubeck,<country>Germany</country>
;</nlm:aff>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<author><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">Insitute of Neurodegenerative Diseases, University of Bordeaux Segalen, Centre National de la Recherche Scientifique Unité Mixte de Recherche 5293, 33076 Bordeaux, France;</nlm:aff>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (metabolism)</term>
<term>Cell Line</term>
<term>Gene Knockdown Techniques</term>
<term>Humans</term>
<term>Lysosomes (metabolism)</term>
<term>Parkinson Disease (enzymology)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Parkinson Disease (pathology)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lysosomes</term>
<term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinson Disease</term>
</keywords>
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<front><div type="abstract" xml:lang="en"><p>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 <italic>ATP13A2</italic>
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.</p>
</div>
</front>
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<country name="Espagne"><noRegion><name sortKey="Martinez Vicente, Marta" sort="Martinez Vicente, Marta" uniqKey="Martinez Vicente M" first="Marta" last="Martinez-Vicente">Marta Martinez-Vicente</name>
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<name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</name>
<name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</name>
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