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
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<author><name sortKey="Andreas, Hartmann" sort="Andreas, Hartmann" uniqKey="Andreas H" first="Hartmann" last="Andreas">Hartmann Andreas</name>
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<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>
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<Month>08</Month>
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<ArticleTitle>Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease.</ArticleTitle>
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<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>
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<ForeName>Lixia</ForeName>
<Initials>L</Initials>
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<ForeName>Franca</ForeName>
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<ForeName>Annekathrin</ForeName>
<Initials>A</Initials>
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<Author ValidYN="Y"><LastName>Roscher</LastName>
<ForeName>René</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Actelion Pharmaceuticals Ltd, 4123 Allschwil, Switzerland.</Affiliation>
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<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>
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<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>
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<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>
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<Author ValidYN="Y"><LastName>Alvarez-Fischer</LastName>
<ForeName>Daniel</ForeName>
<Initials>D</Initials>
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<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. Electronic address: andreas.hartmann@psl.aphp.fr.</Affiliation>
</AffiliationInfo>
</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>2015</Year>
<Month>06</Month>
<Day>17</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>J Neurol Sci</MedlineTA>
<NlmUniqueID>0375403</NlmUniqueID>
<ISSNLinking>0022-510X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D065089">Glycoside Hydrolase Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006649">Histocompatibility Antigens</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>19130-96-2</RegistryNumber>
<NameOfSubstance UI="D017485">1-Deoxynojirimycin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>4L6452S749</RegistryNumber>
<NameOfSubstance UI="D007294">Inositol</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9P21XSP91P</RegistryNumber>
<NameOfSubstance UI="D015632">1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>ADN3S497AZ</RegistryNumber>
<NameOfSubstance UI="C059896">miglustat</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.1.1.27</RegistryNumber>
<NameOfSubstance UI="D007770">L-Lactate Dehydrogenase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.14.16.2</RegistryNumber>
<NameOfSubstance UI="D014446">Tyrosine 3-Monooxygenase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>NHM754Q310</RegistryNumber>
<NameOfSubstance UI="C011423">conduritol epoxide</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D017485" MajorTopicYN="N">1-Deoxynojirimycin</DescriptorName>
<QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName>
<QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015632" MajorTopicYN="N">1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002452" MajorTopicYN="N">Cell Count</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004622" MajorTopicYN="N">Embryo, Mammalian</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005776" MajorTopicYN="N">Gaucher Disease</DescriptorName>
<QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName>
<QualifierName UI="Q000209" MajorTopicYN="Y">etiology</QualifierName>
<QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D065089" MajorTopicYN="N">Glycoside Hydrolase Inhibitors</DescriptorName>
<QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006649" MajorTopicYN="N">Histocompatibility Antigens</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007294" MajorTopicYN="N">Inositol</DescriptorName>
<QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007770" MajorTopicYN="N">L-Lactate Dehydrogenase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008636" MajorTopicYN="N">Mesencephalon</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D028361" MajorTopicYN="N">Mitochondrial Diseases</DescriptorName>
<QualifierName UI="Q000209" MajorTopicYN="Y">etiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020734" MajorTopicYN="N">Parkinsonian Disorders</DescriptorName>
<QualifierName UI="Q000150" MajorTopicYN="Y">complications</QualifierName>
<QualifierName UI="Q000517" MajorTopicYN="N">prevention & control</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014446" MajorTopicYN="N">Tyrosine 3-Monooxygenase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Dopamine cell death</Keyword>
<Keyword MajorTopicYN="N">Gaucher 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>
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