Lysosomal impairment in Parkinson's disease.
Identifieur interne : 000940 ( PubMed/Checkpoint ); précédent : 000939; suivant : 000941Lysosomal impairment in Parkinson's disease.
Auteurs : Benjamin Dehay [France] ; Marta Martinez-Vicente ; Guy A. Caldwell ; Kim A. Caldwell ; Zhenyue Yue ; Mark R. Cookson ; Christine Klein ; Miquel Vila ; Erwan BezardSource :
- Movement disorders : official journal of the Movement Disorder Society [ 1531-8257 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Autophagy, Gaucher Disease (complications), Gaucher Disease (genetics), Gaucher Disease (pathology), Glucosylceramidase (genetics), Glucosylceramidase (metabolism), Humans, Lysosomes (metabolism), Lysosomes (pathology), Parkinson Disease (complications), Parkinson Disease (genetics), Parkinson Disease (pathology), Protein Kinases (genetics), Protein Kinases (metabolism), Protein-Serine-Threonine Kinases (genetics), Proton-Translocating ATPases (genetics), Signal Transduction (physiology).
- MESH :
- chemical , genetics : Glucosylceramidase, Protein Kinases, Protein-Serine-Threonine Kinases, Proton-Translocating ATPases.
- complications : Gaucher Disease, Parkinson Disease.
- genetics : Gaucher Disease, Parkinson Disease.
- chemical , metabolism : Glucosylceramidase, Lysosomes, Protein Kinases.
- pathology : Gaucher Disease, Lysosomes, Parkinson Disease.
- physiology : Signal Transduction.
- Animals, Autophagy, Humans.
Abstract
Impairment of autophagy-lysosomal pathways (ALPs) is increasingly regarded as a major pathogenic event in neurodegenerative diseases, including Parkinson's disease (PD). ALP alterations are observed in sporadic PD brains and in toxic and genetic rodent models of PD-related neurodegeneration. In addition, PD-linked mutations and post-translational modifications of α-synuclein impair its own lysosomal-mediated degradation, thereby contributing to its accumulation and aggregation. Furthermore, other PD-related genes, such as leucine-rich repeat kinase-2 (LRRK2), parkin, and phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1), have been mechanistically linked to alterations in ALPs. Conversely, mutations in lysosomal-related genes, such as glucocerebrosidase (GBA) and lysosomal type 5 P-type ATPase (ATP13A2), have been linked to PD. New data offer mechanistic molecular evidence for such a connection, unraveling a causal link between lysosomal impairment, α-synuclein accumulation, and neurotoxicity. First, PD-related GBA deficiency/mutations initiate a positive feedback loop in which reduced lysosomal function leads to α-synuclein accumulation, which, in turn, further decreases lysosomal GBA activity by impairing the trafficking of GBA from the endoplasmic reticulum-Golgi to lysosomes, leading to neurodegeneration. Second, PD-related mutations/deficiency in the ATP13A2 gene lead to a general lysosomal impairment characterized by lysosomal membrane instability, impaired lysosomal acidification, decreased processing of lysosomal enzymes, reduced degradation of lysosomal substrates, and diminished clearance of autophagosomes, collectively contributing to α-synuclein accumulation and cell death. According to these new findings, primary lysosomal defects could potentially account for Lewy body formation and neurodegeneration in PD, laying the groundwork for the prospective development of new neuroprotective/disease-modifying therapeutic strategies aimed at restoring lysosomal levels and function.
DOI: 10.1002/mds.25462
PubMed: 23580333
Affiliations:
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Caldwell</name></author><author><name sortKey="Caldwell, Kim A" sort="Caldwell, Kim A" uniqKey="Caldwell K" first="Kim A" last="Caldwell">Kim A. Caldwell</name></author><author><name sortKey="Yue, Zhenyue" sort="Yue, Zhenyue" uniqKey="Yue Z" first="Zhenyue" last="Yue">Zhenyue Yue</name></author><author><name sortKey="Cookson, Mark R" sort="Cookson, Mark R" uniqKey="Cookson M" first="Mark R" last="Cookson">Mark R. 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Caldwell</name></author><author><name sortKey="Caldwell, Kim A" sort="Caldwell, Kim A" uniqKey="Caldwell K" first="Kim A" last="Caldwell">Kim A. Caldwell</name></author><author><name sortKey="Yue, Zhenyue" sort="Yue, Zhenyue" uniqKey="Yue Z" first="Zhenyue" last="Yue">Zhenyue Yue</name></author><author><name sortKey="Cookson, Mark R" sort="Cookson, Mark R" uniqKey="Cookson M" first="Mark R" last="Cookson">Mark R. Cookson</name></author><author><name sortKey="Klein, Christine" sort="Klein, Christine" uniqKey="Klein C" first="Christine" last="Klein">Christine Klein</name></author><author><name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</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">Movement disorders : official journal of the Movement Disorder Society</title><idno type="eISSN">1531-8257</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Autophagy</term><term>Gaucher Disease (complications)</term><term>Gaucher Disease (genetics)</term><term>Gaucher Disease (pathology)</term><term>Glucosylceramidase (genetics)</term><term>Glucosylceramidase (metabolism)</term><term>Humans</term><term>Lysosomes (metabolism)</term><term>Lysosomes (pathology)</term><term>Parkinson Disease (complications)</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (pathology)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Proton-Translocating ATPases (genetics)</term><term>Signal Transduction (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glucosylceramidase</term><term>Protein Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Proton-Translocating ATPases</term></keywords><keywords scheme="MESH" qualifier="complications" xml:lang="en"><term>Gaucher Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Gaucher Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucosylceramidase</term><term>Lysosomes</term><term>Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Gaucher Disease</term><term>Lysosomes</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Autophagy</term><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Impairment of autophagy-lysosomal pathways (ALPs) is increasingly regarded as a major pathogenic event in neurodegenerative diseases, including Parkinson's disease (PD). ALP alterations are observed in sporadic PD brains and in toxic and genetic rodent models of PD-related neurodegeneration. In addition, PD-linked mutations and post-translational modifications of α-synuclein impair its own lysosomal-mediated degradation, thereby contributing to its accumulation and aggregation. Furthermore, other PD-related genes, such as leucine-rich repeat kinase-2 (LRRK2), parkin, and phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1), have been mechanistically linked to alterations in ALPs. Conversely, mutations in lysosomal-related genes, such as glucocerebrosidase (GBA) and lysosomal type 5 P-type ATPase (ATP13A2), have been linked to PD. New data offer mechanistic molecular evidence for such a connection, unraveling a causal link between lysosomal impairment, α-synuclein accumulation, and neurotoxicity. First, PD-related GBA deficiency/mutations initiate a positive feedback loop in which reduced lysosomal function leads to α-synuclein accumulation, which, in turn, further decreases lysosomal GBA activity by impairing the trafficking of GBA from the endoplasmic reticulum-Golgi to lysosomes, leading to neurodegeneration. Second, PD-related mutations/deficiency in the ATP13A2 gene lead to a general lysosomal impairment characterized by lysosomal membrane instability, impaired lysosomal acidification, decreased processing of lysosomal enzymes, reduced degradation of lysosomal substrates, and diminished clearance of autophagosomes, collectively contributing to α-synuclein accumulation and cell death. According to these new findings, primary lysosomal defects could potentially account for Lewy body formation and neurodegeneration in PD, laying the groundwork for the prospective development of new neuroprotective/disease-modifying therapeutic strategies aimed at restoring lysosomal levels and function.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">23580333</PMID><DateCreated><Year>2013</Year><Month>06</Month><Day>26</Day></DateCreated><DateCompleted><Year>2014</Year><Month>01</Month><Day>30</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1531-8257</ISSN><JournalIssue CitedMedium="Internet"><Volume>28</Volume><Issue>6</Issue><PubDate><Year>2013</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Movement disorders : official journal of the Movement Disorder Society</Title><ISOAbbreviation>Mov. Disord.</ISOAbbreviation></Journal><ArticleTitle>Lysosomal impairment in Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>725-32</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/mds.25462</ELocationID><Abstract><AbstractText>Impairment of autophagy-lysosomal pathways (ALPs) is increasingly regarded as a major pathogenic event in neurodegenerative diseases, including Parkinson's disease (PD). ALP alterations are observed in sporadic PD brains and in toxic and genetic rodent models of PD-related neurodegeneration. In addition, PD-linked mutations and post-translational modifications of α-synuclein impair its own lysosomal-mediated degradation, thereby contributing to its accumulation and aggregation. Furthermore, other PD-related genes, such as leucine-rich repeat kinase-2 (LRRK2), parkin, and phosphatase and tensin homolog (PTEN)-induced putative kinase 1 (PINK1), have been mechanistically linked to alterations in ALPs. Conversely, mutations in lysosomal-related genes, such as glucocerebrosidase (GBA) and lysosomal type 5 P-type ATPase (ATP13A2), have been linked to PD. New data offer mechanistic molecular evidence for such a connection, unraveling a causal link between lysosomal impairment, α-synuclein accumulation, and neurotoxicity. First, PD-related GBA deficiency/mutations initiate a positive feedback loop in which reduced lysosomal function leads to α-synuclein accumulation, which, in turn, further decreases lysosomal GBA activity by impairing the trafficking of GBA from the endoplasmic reticulum-Golgi to lysosomes, leading to neurodegeneration. Second, PD-related mutations/deficiency in the ATP13A2 gene lead to a general lysosomal impairment characterized by lysosomal membrane instability, impaired lysosomal acidification, decreased processing of lysosomal enzymes, reduced degradation of lysosomal substrates, and diminished clearance of autophagosomes, collectively contributing to α-synuclein accumulation and cell death. According to these new findings, primary lysosomal defects could potentially account for Lewy body formation and neurodegeneration in PD, laying the groundwork for the prospective development of new neuroprotective/disease-modifying therapeutic strategies aimed at restoring lysosomal levels and function.</AbstractText><CopyrightInformation>Copyright © 2013 Movement Disorder Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dehay</LastName><ForeName>Benjamin</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institute of Neurodegenerative Diseases, University of Bordeaux Segalen, Centre National de Recherche Scientifique Unité Mixte de Recherche 5293, Bordeaux, France. benjamin.dehay@u-bordeaux2.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martinez-Vicente</LastName><ForeName>Marta</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Caldwell</LastName><ForeName>Guy 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PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>1</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="doi">10.1002/mds.25462</ArticleId><ArticleId IdType="pubmed">23580333</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><settlement><li>Bordeaux</li></settlement></list><tree><noCountry><name sortKey="Bezard, Erwan" sort="Bezard, Erwan" uniqKey="Bezard E" first="Erwan" last="Bezard">Erwan Bezard</name><name sortKey="Caldwell, Guy A" sort="Caldwell, Guy A" uniqKey="Caldwell G" first="Guy A" last="Caldwell">Guy A. Caldwell</name><name sortKey="Caldwell, Kim A" sort="Caldwell, Kim A" uniqKey="Caldwell K" first="Kim A" last="Caldwell">Kim A. Caldwell</name><name sortKey="Cookson, Mark R" sort="Cookson, Mark R" uniqKey="Cookson M" first="Mark R" last="Cookson">Mark R. Cookson</name><name sortKey="Klein, Christine" sort="Klein, Christine" uniqKey="Klein C" first="Christine" last="Klein">Christine Klein</name><name sortKey="Martinez Vicente, Marta" sort="Martinez Vicente, Marta" uniqKey="Martinez Vicente M" first="Marta" last="Martinez-Vicente">Marta Martinez-Vicente</name><name sortKey="Vila, Miquel" sort="Vila, Miquel" uniqKey="Vila M" first="Miquel" last="Vila">Miquel Vila</name><name sortKey="Yue, Zhenyue" sort="Yue, Zhenyue" uniqKey="Yue Z" first="Zhenyue" last="Yue">Zhenyue Yue</name></noCountry><country name="France"><noRegion><name sortKey="Dehay, Benjamin" sort="Dehay, Benjamin" uniqKey="Dehay B" first="Benjamin" last="Dehay">Benjamin Dehay</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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