Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration.
Identifieur interne : 000860 ( PubMed/Corpus ); précédent : 000859; suivant : 000861Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration.
Auteurs : Benjamin Dehay ; Alfredo Ramirez ; Marta Martinez-Vicente ; Celine Perier ; Marie-Hélène Canron ; Evelyne Doudnikoff ; Anne Vital ; Miquel Vila ; Christine Klein ; Erwan BezardSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 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 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.
DOI: 10.1073/pnas.1112368109
PubMed: 22647602
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pubmed:22647602Le document en format XML
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uniqKey="Perier C" first="Celine" last="Perier">Celine Perier</name></author><author><name sortKey="Canron, Marie Helene" sort="Canron, Marie Helene" uniqKey="Canron M" first="Marie-Hélène" last="Canron">Marie-Hélène Canron</name></author><author><name sortKey="Doudnikoff, Evelyne" sort="Doudnikoff, Evelyne" uniqKey="Doudnikoff E" first="Evelyne" last="Doudnikoff">Evelyne Doudnikoff</name></author><author><name sortKey="Vital, Anne" sort="Vital, Anne" uniqKey="Vital A" first="Anne" last="Vital">Anne Vital</name></author><author><name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</name></author><author><name sortKey="Klein, Christine" sort="Klein, Christine" uniqKey="Klein C" first="Christine" last="Klein">Christine Klein</name></author><author><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name></author></titleStmt><publicationStmt><idno 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sort="Ramirez, Alfredo" uniqKey="Ramirez A" first="Alfredo" last="Ramirez">Alfredo Ramirez</name></author><author><name sortKey="Martinez Vicente, Marta" sort="Martinez Vicente, Marta" uniqKey="Martinez Vicente M" first="Marta" last="Martinez-Vicente">Marta Martinez-Vicente</name></author><author><name sortKey="Perier, Celine" sort="Perier, Celine" uniqKey="Perier C" first="Celine" last="Perier">Celine Perier</name></author><author><name sortKey="Canron, Marie Helene" sort="Canron, Marie Helene" uniqKey="Canron M" first="Marie-Hélène" last="Canron">Marie-Hélène Canron</name></author><author><name sortKey="Doudnikoff, Evelyne" sort="Doudnikoff, Evelyne" uniqKey="Doudnikoff E" first="Evelyne" last="Doudnikoff">Evelyne Doudnikoff</name></author><author><name sortKey="Vital, Anne" sort="Vital, Anne" uniqKey="Vital A" first="Anne" last="Vital">Anne Vital</name></author><author><name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</name></author><author><name sortKey="Klein, Christine" sort="Klein, Christine" uniqKey="Klein C" first="Christine" last="Klein">Christine Klein</name></author><author><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><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></keywords><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><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Gene Knockdown Techniques</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22647602</PMID><DateCreated><Year>2012</Year><Month>06</Month><Day>13</Day></DateCreated><DateCompleted><Year>2012</Year><Month>08</Month><Day>28</Day></DateCompleted><DateRevised><Year>2015</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>109</Volume><Issue>24</Issue><PubDate><Year>2012</Year><Month>Jun</Month><Day>12</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration.</ArticleTitle><Pagination><MedlinePgn>9611-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1112368109</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dehay</LastName><ForeName>Benjamin</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Insitute of Neurodegenerative Diseases, University of Bordeaux Segalen, Centre National de la Recherche Scientifique Unité Mixte de Recherche 5293, 33076 Bordeaux, France. benjamin.dehay@u-bordeaux2.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ramirez</LastName><ForeName>Alfredo</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Martinez-Vicente</LastName><ForeName>Marta</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Perier</LastName><ForeName>Celine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Canron</LastName><ForeName>Marie-Hélène</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Doudnikoff</LastName><ForeName>Evelyne</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Vital</LastName><ForeName>Anne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Vila</LastName><ForeName>Miquel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Klein</LastName><ForeName>Christine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Bezard</LastName><ForeName>Erwan</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>05</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>PLoS Genet. 2010 Jul;6(7):e1001026</RefSource><PMID Version="1">20664788</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2010 Jun;113(5):1263-74</RefSource><PMID Version="1">20345754</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Acta Neuropathol. 2010 Nov;120(5):641-9</RefSource><PMID Version="1">20838799</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2011 Jan;7(1):98-100</RefSource><PMID Version="1">21045565</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurobiol Dis. 2011 Jun;42(3):360-7</RefSource><PMID Version="1">21303699</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mov Disord. 2011 May;26(6):1049-55</RefSource><PMID Version="1">21626550</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mov Disord. 2011 May;26(6):1056-71</RefSource><PMID Version="1">21626551</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cell. 2011 Jul 8;146(1):37-52</RefSource><PMID Version="1">21700325</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Rev Neurosci. 2011 Aug;12(8):437-52</RefSource><PMID Version="1">21772323</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Hum Mutat. 2011 Aug;32(8):956-64</RefSource><PMID Version="1">21542062</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2011 Aug 12;286(32):28080-8</RefSource><PMID Version="1">21653695</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cell Death Differ. 2011 Sep;18(9):1425-33</RefSource><PMID Version="1">21566660</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2011 Sep 15;20(18):3565-77</RefSource><PMID Version="1">21665991</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Annu Rev Genomics Hum Genet. 2011;12:301-25</RefSource><PMID Version="1">21639795</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Clin Genet. 2012 Sep;82(3):256-63</RefSource><PMID Version="1">21696388</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2010 Sep 15;30(37):12535-44</RefSource><PMID Version="1">20844148</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2003 Jul 4;278(27):25009-13</RefSource><PMID Version="1">12719433</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Membr Biol. 2003 Apr-Jun;20(2):141-54</RefSource><PMID Version="1">12851071</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuron. 2003 Sep 11;39(6):889-909</RefSource><PMID Version="1">12971891</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Science. 2004 Aug 27;305(5688):1292-5</RefSource><PMID Version="1">15333840</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2004 Sep 17;279(38):39982-8</RefSource><PMID Version="1">15258139</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Acta Neurol Scand. 1994 May;89(5):347-52</RefSource><PMID Version="1">8085432</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>N Engl J Med. 2004 Nov 4;351(19):1972-7</RefSource><PMID Version="1">15525722</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Genet. 2006 Oct;38(10):1184-91</RefSource><PMID Version="1">16964263</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurology. 2007 May 8;68(19):1557-62</RefSource><PMID Version="1">17485642</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Rev Mol Cell Biol. 2007 Aug;8(8):622-32</RefSource><PMID Version="1">17637737</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Clin Invest. 2008 Feb;118(2):777-88</RefSource><PMID Version="1">18172548</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2008 Jul;106(1):24-36</RefSource><PMID Version="1">18384642</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 2008 Sep 9;47(36):9678-87</RefSource><PMID Version="1">18702517</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Oncogene. 2008 Oct 27;27(50):6434-51</RefSource><PMID Version="1">18955971</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nat Genet. 2009 Mar;41(3):308-15</RefSource><PMID Version="1">19182805</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 2009 Apr;1793(4):636-49</RefSource><PMID Version="1">19146888</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochem Biophys Res Commun. 2009 May 29;383(2):198-202</RefSource><PMID Version="1">19345671</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2009 Jul;5(5):585-9</RefSource><PMID Version="1">19411822</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neurobiol Dis. 2009 Sep;35(3):385-98</RefSource><PMID Version="1">19505575</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2010 Apr 30;285(18):13621-9</RefSource><PMID Version="1">20200163</PMID></CommentsCorrections><CommentsCorrections RefType="CommentIn"><RefSource>Mov Disord. 2012 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