Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in α-synuclein transgenic mice
Identifieur interne : 000C62 ( Main/Exploration ); précédent : 000C61; suivant : 000C63Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in α-synuclein transgenic mice
Auteurs : Margot Fournier [France] ; Amandine Roux [France] ; Jérôme Garrigue [France] ; Marie-Paule Muriel [France] ; Paul Blanche ; Hilal A. Lashuel ; John P. Anderson [États-Unis] ; Robin Barbour [États-Unis] ; Jiping Huang [États-Unis] ; Sophie Tezenas Du Montcel ; Alexis Brice [France] ; Olga Corti [France]Source :
- BMC Neuroscience [ 1471-2202 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Blotting, Western, Brain (metabolism), Brain (pathology), Disease Models, Animal, Fluorescent Antibody Technique, Humans, Mass Spectrometry, Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Microscopy, Electron, Transmission, Motor Skills, Nerve Degeneration (genetics), Nerve Degeneration (pathology), Parkinson Disease (genetics), Parkinson Disease (pathology), Ubiquitin-Protein Ligases (genetics), alpha-Synuclein (genetics).
- MESH :
- chemical , genetics : Ubiquitin-Protein Ligases, alpha-Synuclein.
- genetics : Nerve Degeneration, Parkinson Disease.
- metabolism : Brain.
- pathology : Brain, Nerve Degeneration, Parkinson Disease.
- Animals, Blotting, Western, Disease Models, Animal, Fluorescent Antibody Technique, Humans, Mass Spectrometry, Mice, Mice, Inbred C57BL, Mice, Knockout, Mice, Transgenic, Microscopy, Electron, Transmission, Motor Skills.
- mix :
Abstract
Mutations of the gene encoding the major component of Lewy bodies (LB), α-synuclein (α-syn), cause autosomal dominant forms of Parkinson’s disease (PD), whereas loss-of-function mutations of the gene encoding the multifunctional E3 ubiquitin-protein ligase Parkin account for autosomal recessive forms of the disease. Parkin overproduction protects against α-syn-dependent neurodegeneration in various
Longitudinal behavioral follow-up of these mice indicated that Parkin depletion delayed disease-predictive sensorimotor impairment due to α-syn accumulation, in a dose-dependent fashion. At the end stage of the disease, neuronal deposits containing fibrillar α-syn species phosphorylated at S129 (PS129α-syn) were the predominant neuropathological feature in hA30Pα-syn mice, regardless of their
These findings suggest that Parkin deficiency acts as a protective modifier in α-syn-dependent neurodegeneration, without overtly affecting the composition and characteristics of α-syn deposits in end-stage disease.
Url:
DOI: 10.1186/1471-2202-14-135
PubMed: 24192137
PubMed Central: 4228309
Affiliations:
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Le document en format XML
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Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne, Lausanne CH-1015 Switzerland</nlm:aff><wicri:noCountry code="subfield">Lausanne CH-1015 Switzerland</wicri:noCountry></affiliation><affiliation><nlm:aff id="I9">Current address: Center for Psychiatric Neuroscience, Department of Psychiatry, Lausanne University Hospital, Prilly-Lausanne, CH 1008 Switzerland</nlm:aff><wicri:noCountry code="subfield">CH 1008 Switzerland</wicri:noCountry></affiliation></author><author><name sortKey="Roux, Amandine" sort="Roux, Amandine" uniqKey="Roux A" first="Amandine" last="Roux">Amandine Roux</name><affiliation wicri:level="3"><nlm:aff id="I1">Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement 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Pitié-Salpêtrière, F-75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I2">UPMC Université Paris 06, UMR_S975, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>UPMC Université Paris 06, UMR_S975, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I3">CNRS, UMR 7225, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>CNRS, UMR 7225, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Muriel, Marie Paule" sort="Muriel, Marie Paule" uniqKey="Muriel M" first="Marie-Paule" last="Muriel">Marie-Paule Muriel</name><affiliation wicri:level="3"><nlm:aff id="I1">Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I2">UPMC Université Paris 06, UMR_S975, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>UPMC Université Paris 06, UMR_S975, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement 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Lashuel</name><affiliation><nlm:aff id="I4">Laboratory of Molecular Neurobiology and Chemical Biology of Neurodegeneration, Brain Mind Institute, Ecole Polytechnique Fédérale de Lausanne, Lausanne CH-1015 Switzerland</nlm:aff><wicri:noCountry code="subfield">Lausanne CH-1015 Switzerland</wicri:noCountry></affiliation></author><author><name sortKey="Anderson, John P" sort="Anderson, John P" uniqKey="Anderson J" first="John P" last="Anderson">John P. Anderson</name><affiliation wicri:level="2"><nlm:aff id="I6">Elan Pharmaceuticals, 180 Oyster Point Blvd, South San Francisco, California, CA 94080 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Elan Pharmaceuticals, 180 Oyster Point Blvd, South San Francisco, California</wicri:cityArea></affiliation></author><author><name sortKey="Barbour, Robin" sort="Barbour, Robin" uniqKey="Barbour R" first="Robin" last="Barbour">Robin Barbour</name><affiliation wicri:level="2"><nlm:aff id="I6">Elan Pharmaceuticals, 180 Oyster Point Blvd, South San Francisco, California, CA 94080 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Elan Pharmaceuticals, 180 Oyster Point Blvd, South San Francisco, California</wicri:cityArea></affiliation></author><author><name sortKey="Huang, Jiping" sort="Huang, Jiping" uniqKey="Huang J" first="Jiping" last="Huang">Jiping Huang</name><affiliation wicri:level="2"><nlm:aff id="I6">Elan Pharmaceuticals, 180 Oyster Point Blvd, South San Francisco, California, CA 94080 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Elan Pharmaceuticals, 180 Oyster Point Blvd, South San Francisco, California</wicri:cityArea></affiliation></author><author><name sortKey="Du Montcel, Sophie Tezenas" sort="Du Montcel, Sophie Tezenas" uniqKey="Du Montcel S" first="Sophie Tezenas" last="Du Montcel">Sophie Tezenas Du Montcel</name><affiliation><nlm:aff id="I5">Université Pierre et Marie Curie-Paris 6, ER4 Modeling in Clinical Research, Paris F-75013 France</nlm:aff><wicri:noCountry code="subfield">Paris F-75013 France</wicri:noCountry></affiliation><affiliation><nlm:aff id="I7">Department of Biostatistics and Medical Informatics, Hôpital de la Pitié-Salpêtrière, Assistance Publique-Hôpitaux, 47 Boulevard de l'Hôpital, Paris F-75013 France</nlm:aff><wicri:noCountry code="subfield">Paris F-75013 France</wicri:noCountry></affiliation></author><author><name sortKey="Brice, Alexis" sort="Brice, Alexis" uniqKey="Brice A" first="Alexis" last="Brice">Alexis Brice</name><affiliation wicri:level="3"><nlm:aff id="I1">Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I2">UPMC Université Paris 06, UMR_S975, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>UPMC Université Paris 06, UMR_S975, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I3">CNRS, UMR 7225, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>CNRS, UMR 7225, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I8">AP-HP, Hôpital de la Salpêtrière, Department of Genetics and Cytogenetics, F-75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>AP-HP, Hôpital de la Salpêtrière, Department of Genetics and Cytogenetics, F-75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Corti, Olga" sort="Corti, Olga" uniqKey="Corti O" first="Olga" last="Corti">Olga Corti</name><affiliation wicri:level="3"><nlm:aff id="I1">Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U 975, CRICM, Hôpital de la Pitié-Salpêtrière, F-75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I2">UPMC Université Paris 06, UMR_S975, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>UPMC Université Paris 06, UMR_S975, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I3">CNRS, UMR 7225, F-75013, Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>CNRS, UMR 7225, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author></analytic><series><title level="j">BMC Neuroscience</title><idno type="eISSN">1471-2202</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Brain (metabolism)</term><term>Brain (pathology)</term><term>Disease Models, Animal</term><term>Fluorescent Antibody Technique</term><term>Humans</term><term>Mass Spectrometry</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Mice, Knockout</term><term>Mice, Transgenic</term><term>Microscopy, Electron, Transmission</term><term>Motor Skills</term><term>Nerve Degeneration (genetics)</term><term>Nerve Degeneration (pathology)</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (pathology)</term><term>Ubiquitin-Protein Ligases (genetics)</term><term>alpha-Synuclein (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ubiquitin-Protein Ligases</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Nerve Degeneration</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Brain</term><term>Nerve Degeneration</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Disease Models, Animal</term><term>Fluorescent Antibody Technique</term><term>Humans</term><term>Mass Spectrometry</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Mice, Knockout</term><term>Mice, Transgenic</term><term>Microscopy, Electron, Transmission</term><term>Motor Skills</term></keywords><keywords scheme="mix" xml:lang="en"><term>Parkinson's disease</term><term>Posttranslational modifications</term><term>Transgenic mice overproducing α-syn</term><term>Ubiquitin</term><term>parkin knockout mice</term><term>α-syn phosphorylation</term><term>α-syn truncation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>Mutations of the gene encoding the major component of Lewy bodies (LB), α-synuclein (α-syn), cause autosomal dominant forms of Parkinson’s disease (PD), whereas loss-of-function mutations of the gene encoding the multifunctional E3 ubiquitin-protein ligase Parkin account for autosomal recessive forms of the disease. Parkin overproduction protects against α-syn-dependent neurodegeneration in various <italic>in vitro</italic> and <italic>in vivo</italic> models, but it remains unclear whether this process is affected by Parkin deficiency. We addressed this issue, by carrying out more detailed analyses of transgenic mice overproducing the A30P variant of human α-syn (hA30Pα-syn) and with two, one or no <italic>parkin</italic> knockout alleles.</p></sec><sec><title>Results</title><p>Longitudinal behavioral follow-up of these mice indicated that Parkin depletion delayed disease-predictive sensorimotor impairment due to α-syn accumulation, in a dose-dependent fashion. At the end stage of the disease, neuronal deposits containing fibrillar α-syn species phosphorylated at S129 (P<sup>S129</sup>α-syn) were the predominant neuropathological feature in hA30Pα-syn mice, regardless of their <italic>parkin</italic> expression. Some of these deposits colocalized with the LB markers ubiquitin and α-syn truncated at D135 (α-synD135), indicating that P<sup>S129</sup>α-syn is subjected to secondary posttranslational modification (PTM); these features were not significantly affected by <italic>parkin</italic> dysfunction.</p></sec><sec><title>Conclusions</title><p>These findings suggest that Parkin deficiency acts as a protective modifier in α-syn-dependent neurodegeneration, without overtly affecting the composition and characteristics of α-syn deposits in end-stage disease.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Oueslati, A" uniqKey="Oueslati A">A Oueslati</name></author><author><name sortKey="Fournier, M" uniqKey="Fournier M">M Fournier</name></author><author><name sortKey="Lashuel, Ha" uniqKey="Lashuel H">HA Lashuel</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Anderson, Jp" uniqKey="Anderson J">JP 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Zharkovsky</name></author><author><name sortKey="Kaasik, A" uniqKey="Kaasik A">A Kaasik</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>France</li><li>États-Unis</li></country><region><li>Californie</li><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><noCountry><name sortKey="Blanche, Paul" sort="Blanche, Paul" uniqKey="Blanche P" first="Paul" last="Blanche">Paul Blanche</name><name sortKey="Du Montcel, Sophie Tezenas" sort="Du Montcel, Sophie Tezenas" uniqKey="Du Montcel S" first="Sophie Tezenas" last="Du Montcel">Sophie Tezenas Du Montcel</name><name sortKey="Lashuel, Hilal A" sort="Lashuel, Hilal A" uniqKey="Lashuel H" first="Hilal A" last="Lashuel">Hilal A. 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Anderson</name></region><name sortKey="Barbour, Robin" sort="Barbour, Robin" uniqKey="Barbour R" first="Robin" last="Barbour">Robin Barbour</name><name sortKey="Huang, Jiping" sort="Huang, Jiping" uniqKey="Huang J" first="Jiping" last="Huang">Jiping Huang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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