Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease.
Identifieur interne : 000298 ( PubMed/Corpus ); précédent : 000297; suivant : 000299Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease.
Auteurs : Carmen Noelker ; Lixia Lu ; Matthias Höllerhage ; Franca Vulinovic ; Annekathrin Sturn ; René Roscher ; Günter U. Höglinger ; Etienne C. Hirsch ; Wolfgang H. Oertel ; Daniel Alvarez-Fischer ; Hartmann AndreasSource :
- Journal of the neurological sciences [ 1878-5883 ] ; 2015.
English descriptors
- KwdEn :
- 1-Deoxynojirimycin (analogs & derivatives), 1-Deoxynojirimycin (therapeutic use), 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (pharmacology), Animals, Brain (drug effects), Brain (metabolism), Brain (pathology), Cell Count, Cells, Cultured, Disease Models, Animal, Embryo, Mammalian, Gaucher Disease (drug therapy), Gaucher Disease (etiology), Gaucher Disease (prevention & control), Glycoside Hydrolase Inhibitors (therapeutic use), Histocompatibility Antigens (metabolism), Inositol (analogs & derivatives), Inositol (metabolism), L-Lactate Dehydrogenase (metabolism), Male, Mesencephalon (metabolism), Mice, Mice, Inbred C57BL, Mitochondrial Diseases (etiology), Neurons (drug effects), Neurons (metabolism), Parkinsonian Disorders (complications), Parkinsonian Disorders (prevention & control), Tyrosine 3-Monooxygenase (metabolism).
- MESH :
- chemical , analogs & derivatives : 1-Deoxynojirimycin, Inositol.
- chemical , metabolism : Histocompatibility Antigens, Inositol, L-Lactate Dehydrogenase, Tyrosine 3-Monooxygenase.
- chemical , pharmacology : 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine.
- chemical , therapeutic use : 1-Deoxynojirimycin, Glycoside Hydrolase Inhibitors.
- complications : Parkinsonian Disorders.
- drug effects : Brain, Neurons.
- drug therapy : Gaucher Disease.
- etiology : Gaucher Disease, Mitochondrial Diseases.
- metabolism : Brain, Mesencephalon, Neurons.
- pathology : Brain.
- prevention & control : Gaucher Disease, Parkinsonian Disorders.
- Animals, Cell Count, Cells, Cultured, Disease Models, Animal, Embryo, Mammalian, Male, Mice, Mice, Inbred C57BL.
Abstract
Gaucher disease is an autosomal recessive disease, caused by a lack or functional deficiency of the lysosomal enzyme, glucocerebrosidase (GCase). Recently, mutations in the glucocerebrosidase gene (GBA) have been associated with Parkinson's disease (PD) and GBA mutations are now considered the most important genetic vulnerability factor for PD. In this study, we have investigated (i) in vivo whether inhibition of the enzyme glucosylceramide synthase by miglustat may protect C57Bl/6 mice against subchronic 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) intoxication and (ii) in vitro whether a decrease of GCase activity may render dopaminergic neurons susceptible to MPP(+) (1-methyl-4-phenylpyridinium) or alpha-synuclein (α-Syn) toxicity and amenable to miglustat treatment. We could demonstrate that reduction of glucocerebroside by inhibition of glucosylceramide synthase partially protects mice against MPTP-induced toxicity. Conversely, we could show that inhibition of GCase activity with conduritol-B-epoxide (CBE) enhances both α-Syn and MPP(+) induced toxicity in vitro. However, only CBE-induced enhancement of MPP(+) toxicity could be reversed by miglustat. Moreover, we were unable to reveal any alterations of complex I activity or cell respiration upon treatment with either CBE or miglustat. Our findings suggest that the reduction of GCase activity rather than an accumulation of glucocerebroside increases aSyn toxicity.
DOI: 10.1016/j.jns.2015.06.030
PubMed: 26104567
Links to Exploration step
pubmed:26104567Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease.</title><author><name sortKey="Noelker, Carmen" sort="Noelker, Carmen" uniqKey="Noelker C" first="Carmen" last="Noelker">Carmen Noelker</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France; Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Lu, Lixia" sort="Lu, Lixia" uniqKey="Lu L" first="Lixia" last="Lu">Lixia Lu</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hollerhage, Matthias" sort="Hollerhage, Matthias" uniqKey="Hollerhage M" first="Matthias" last="Höllerhage">Matthias Höllerhage</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany; Department of Neurology, Technical University, Munich, Germany.; Deptartment of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Vulinovic, Franca" sort="Vulinovic, Franca" uniqKey="Vulinovic F" first="Franca" last="Vulinovic">Franca Vulinovic</name><affiliation><nlm:affiliation>Institute of Neurogenetics, University of Luebeck, 23562 Luebeck, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Sturn, Annekathrin" sort="Sturn, Annekathrin" uniqKey="Sturn A" first="Annekathrin" last="Sturn">Annekathrin Sturn</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Roscher, Rene" sort="Roscher, Rene" uniqKey="Roscher R" first="René" last="Roscher">René Roscher</name><affiliation><nlm:affiliation>Actelion Pharmaceuticals Ltd, 4123 Allschwil, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Hoglinger, Gunter U" sort="Hoglinger, Gunter U" uniqKey="Hoglinger G" first="Günter U" last="Höglinger">Günter U. Höglinger</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany; Department of Neurology, Technical University, Munich, Germany.; Deptartment of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Hirsch, Etienne C" sort="Hirsch, Etienne C" uniqKey="Hirsch E" first="Etienne C" last="Hirsch">Etienne C. Hirsch</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Oertel, Wolfgang H" sort="Oertel, Wolfgang H" uniqKey="Oertel W" first="Wolfgang H" last="Oertel">Wolfgang H. Oertel</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Alvarez Fischer, Daniel" sort="Alvarez Fischer, Daniel" uniqKey="Alvarez Fischer D" first="Daniel" last="Alvarez-Fischer">Daniel Alvarez-Fischer</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France; Institute of Neurogenetics, University of Luebeck, 23562 Luebeck, Germany; Department of Psychiatry, University of Luebeck, 23562 Luebeck, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Andreas, Hartmann" sort="Andreas, Hartmann" uniqKey="Andreas H" first="Hartmann" last="Andreas">Hartmann Andreas</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France. Electronic address: andreas.hartmann@psl.aphp.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26104567</idno><idno type="pmid">26104567</idno><idno type="doi">10.1016/j.jns.2015.06.030</idno><idno type="wicri:Area/PubMed/Corpus">000298</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000298</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease.</title><author><name sortKey="Noelker, Carmen" sort="Noelker, Carmen" uniqKey="Noelker C" first="Carmen" last="Noelker">Carmen Noelker</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France; Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Lu, Lixia" sort="Lu, Lixia" uniqKey="Lu L" first="Lixia" last="Lu">Lixia Lu</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hollerhage, Matthias" sort="Hollerhage, Matthias" uniqKey="Hollerhage M" first="Matthias" last="Höllerhage">Matthias Höllerhage</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany; Department of Neurology, Technical University, Munich, Germany.; Deptartment of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Vulinovic, Franca" sort="Vulinovic, Franca" uniqKey="Vulinovic F" first="Franca" last="Vulinovic">Franca Vulinovic</name><affiliation><nlm:affiliation>Institute of Neurogenetics, University of Luebeck, 23562 Luebeck, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Sturn, Annekathrin" sort="Sturn, Annekathrin" uniqKey="Sturn A" first="Annekathrin" last="Sturn">Annekathrin Sturn</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Roscher, Rene" sort="Roscher, Rene" uniqKey="Roscher R" first="René" last="Roscher">René Roscher</name><affiliation><nlm:affiliation>Actelion Pharmaceuticals Ltd, 4123 Allschwil, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Hoglinger, Gunter U" sort="Hoglinger, Gunter U" uniqKey="Hoglinger G" first="Günter U" last="Höglinger">Günter U. Höglinger</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany; Department of Neurology, Technical University, Munich, Germany.; Deptartment of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Hirsch, Etienne C" sort="Hirsch, Etienne C" uniqKey="Hirsch E" first="Etienne C" last="Hirsch">Etienne C. Hirsch</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Oertel, Wolfgang H" sort="Oertel, Wolfgang H" uniqKey="Oertel W" first="Wolfgang H" last="Oertel">Wolfgang H. Oertel</name><affiliation><nlm:affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Alvarez Fischer, Daniel" sort="Alvarez Fischer, Daniel" uniqKey="Alvarez Fischer D" first="Daniel" last="Alvarez-Fischer">Daniel Alvarez-Fischer</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France; Institute of Neurogenetics, University of Luebeck, 23562 Luebeck, Germany; Department of Psychiatry, University of Luebeck, 23562 Luebeck, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Andreas, Hartmann" sort="Andreas, Hartmann" uniqKey="Andreas H" first="Hartmann" last="Andreas">Hartmann Andreas</name><affiliation><nlm:affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France. Electronic address: andreas.hartmann@psl.aphp.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of the neurological sciences</title><idno type="eISSN">1878-5883</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1-Deoxynojirimycin (analogs & derivatives)</term><term>1-Deoxynojirimycin (therapeutic use)</term><term>1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (pharmacology)</term><term>Animals</term><term>Brain (drug effects)</term><term>Brain (metabolism)</term><term>Brain (pathology)</term><term>Cell Count</term><term>Cells, Cultured</term><term>Disease Models, Animal</term><term>Embryo, Mammalian</term><term>Gaucher Disease (drug therapy)</term><term>Gaucher Disease (etiology)</term><term>Gaucher Disease (prevention & control)</term><term>Glycoside Hydrolase Inhibitors (therapeutic use)</term><term>Histocompatibility Antigens (metabolism)</term><term>Inositol (analogs & derivatives)</term><term>Inositol (metabolism)</term><term>L-Lactate Dehydrogenase (metabolism)</term><term>Male</term><term>Mesencephalon (metabolism)</term><term>Mice</term><term>Mice, Inbred C57BL</term><term>Mitochondrial Diseases (etiology)</term><term>Neurons (drug effects)</term><term>Neurons (metabolism)</term><term>Parkinsonian Disorders (complications)</term><term>Parkinsonian Disorders (prevention & control)</term><term>Tyrosine 3-Monooxygenase (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>1-Deoxynojirimycin</term><term>Inositol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Histocompatibility Antigens</term><term>Inositol</term><term>L-Lactate Dehydrogenase</term><term>Tyrosine 3-Monooxygenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>1-Deoxynojirimycin</term><term>Glycoside Hydrolase Inhibitors</term></keywords><keywords scheme="MESH" qualifier="complications" xml:lang="en"><term>Parkinsonian Disorders</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Brain</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Gaucher Disease</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Gaucher Disease</term><term>Mitochondrial Diseases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term><term>Mesencephalon</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Brain</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Gaucher Disease</term><term>Parkinsonian Disorders</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Count</term><term>Cells, Cultured</term><term>Disease Models, Animal</term><term>Embryo, Mammalian</term><term>Male</term><term>Mice</term><term>Mice, Inbred C57BL</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Gaucher disease is an autosomal recessive disease, caused by a lack or functional deficiency of the lysosomal enzyme, glucocerebrosidase (GCase). Recently, mutations in the glucocerebrosidase gene (GBA) have been associated with Parkinson's disease (PD) and GBA mutations are now considered the most important genetic vulnerability factor for PD. In this study, we have investigated (i) in vivo whether inhibition of the enzyme glucosylceramide synthase by miglustat may protect C57Bl/6 mice against subchronic 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) intoxication and (ii) in vitro whether a decrease of GCase activity may render dopaminergic neurons susceptible to MPP(+) (1-methyl-4-phenylpyridinium) or alpha-synuclein (α-Syn) toxicity and amenable to miglustat treatment. We could demonstrate that reduction of glucocerebroside by inhibition of glucosylceramide synthase partially protects mice against MPTP-induced toxicity. Conversely, we could show that inhibition of GCase activity with conduritol-B-epoxide (CBE) enhances both α-Syn and MPP(+) induced toxicity in vitro. However, only CBE-induced enhancement of MPP(+) toxicity could be reversed by miglustat. Moreover, we were unable to reveal any alterations of complex I activity or cell respiration upon treatment with either CBE or miglustat. Our findings suggest that the reduction of GCase activity rather than an accumulation of glucocerebroside increases aSyn toxicity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26104567</PMID><DateCreated><Year>2015</Year><Month>08</Month><Day>19</Day></DateCreated><DateCompleted><Year>2016</Year><Month>06</Month><Day>17</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-5883</ISSN><JournalIssue CitedMedium="Internet"><Volume>356</Volume><Issue>1-2</Issue><PubDate><Year>2015</Year><Month>Sep</Month><Day>15</Day></PubDate></JournalIssue><Title>Journal of the neurological sciences</Title><ISOAbbreviation>J. Neurol. Sci.</ISOAbbreviation></Journal><ArticleTitle>Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease.</ArticleTitle><Pagination><MedlinePgn>129-36</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jns.2015.06.030</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0022-510X(15)00371-8</ELocationID><Abstract><AbstractText>Gaucher disease is an autosomal recessive disease, caused by a lack or functional deficiency of the lysosomal enzyme, glucocerebrosidase (GCase). Recently, mutations in the glucocerebrosidase gene (GBA) have been associated with Parkinson's disease (PD) and GBA mutations are now considered the most important genetic vulnerability factor for PD. In this study, we have investigated (i) in vivo whether inhibition of the enzyme glucosylceramide synthase by miglustat may protect C57Bl/6 mice against subchronic 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) intoxication and (ii) in vitro whether a decrease of GCase activity may render dopaminergic neurons susceptible to MPP(+) (1-methyl-4-phenylpyridinium) or alpha-synuclein (α-Syn) toxicity and amenable to miglustat treatment. We could demonstrate that reduction of glucocerebroside by inhibition of glucosylceramide synthase partially protects mice against MPTP-induced toxicity. Conversely, we could show that inhibition of GCase activity with conduritol-B-epoxide (CBE) enhances both α-Syn and MPP(+) induced toxicity in vitro. However, only CBE-induced enhancement of MPP(+) toxicity could be reversed by miglustat. Moreover, we were unable to reveal any alterations of complex I activity or cell respiration upon treatment with either CBE or miglustat. Our findings suggest that the reduction of GCase activity rather than an accumulation of glucocerebroside increases aSyn toxicity.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Noelker</LastName><ForeName>Carmen</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France; Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Lixia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Höllerhage</LastName><ForeName>Matthias</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany; Department of Neurology, Technical University, Munich, Germany.; Deptartment of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vulinovic</LastName><ForeName>Franca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institute of Neurogenetics, University of Luebeck, 23562 Luebeck, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sturn</LastName><ForeName>Annekathrin</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roscher</LastName><ForeName>René</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Actelion Pharmaceuticals Ltd, 4123 Allschwil, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Höglinger</LastName><ForeName>Günter U</ForeName><Initials>GU</Initials><AffiliationInfo><Affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany; Department of Neurology, Technical University, Munich, Germany.; Deptartment of Translational Neurodegeneration, German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hirsch</LastName><ForeName>Etienne C</ForeName><Initials>EC</Initials><AffiliationInfo><Affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oertel</LastName><ForeName>Wolfgang H</ForeName><Initials>WH</Initials><AffiliationInfo><Affiliation>Department of Neurology, Faculty of Medicine, Philipps-University, Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alvarez-Fischer</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France; Institute of Neurogenetics, University of Luebeck, 23562 Luebeck, Germany; Department of Psychiatry, University of Luebeck, 23562 Luebeck, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Andreas</LastName><ForeName>Hartmann</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>INSERM, CR-ICM, UMR_S1127, 75013 Paris, France; Université Pierre et Marie Curie Paris 06, UMR_S975, 75013 Paris France; CNRS, UMR 7225, CR-ICM, Groupe Hospitalier Pitié-Salpêtrière, 75013 Paris, France. 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disease</Keyword><Keyword MajorTopicYN="N">Glucocerebrosidase</Keyword><Keyword MajorTopicYN="N">MPTP</Keyword><Keyword MajorTopicYN="N">Mitochondria</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">α-Syn</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>10</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>05</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>06</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>6</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26104567</ArticleId><ArticleId IdType="pii">S0022-510X(15)00371-8</ArticleId><ArticleId IdType="doi">10.1016/j.jns.2015.06.030</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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