Copper pathology in vulnerable brain regions in Parkinson's disease.
Identifieur interne : 000585 ( PubMed/Corpus ); précédent : 000584; suivant : 000586Copper pathology in vulnerable brain regions in Parkinson's disease.
Auteurs : Katherine M. Davies ; Sylvain Bohic ; Asunci N Carmona ; Richard Ortega ; Veronica Cottam ; Dominic J. Hare ; John P M. Finberg ; Stefanie Reyes ; Glenda M. Halliday ; Julian F B. Mercer ; Kay L. DoubleSource :
- Neurobiology of aging [ 1558-1497 ] ; 2014.
English descriptors
- KwdEn :
- Cation Transport Proteins (metabolism), Copper (metabolism), Gyrus Cinguli (enzymology), Humans, Locus Coeruleus (cytology), Locus Coeruleus (metabolism), Molecular Targeted Therapy, Neurons (metabolism), Parkinson Disease (drug therapy), Parkinson Disease (genetics), Parkinson Disease (metabolism), Substantia Nigra (cytology), Substantia Nigra (metabolism), Superoxide Dismutase (metabolism), Superoxide Dismutase-1, alpha-Synuclein.
- MESH :
- chemical , metabolism : Cation Transport Proteins, Copper, Superoxide Dismutase.
- cytology : Locus Coeruleus, Substantia Nigra.
- drug therapy : Parkinson Disease.
- enzymology : Gyrus Cinguli.
- genetics : Parkinson Disease.
- metabolism : Locus Coeruleus, Neurons, Parkinson Disease, Substantia Nigra.
- Humans, Molecular Targeted Therapy, Superoxide Dismutase-1, alpha-Synuclein.
Abstract
Synchrotron-based x-ray fluorescence microscopy, immunofluorescence, and Western blotting were used to investigate changes in copper (Cu) and Cu-associated pathways in the vulnerable substantia nigra (SN) and locus coeruleus (LC) and in nondegenerating brain regions in cases of Parkinson's disease (PD) and appropriate healthy and disease controls. In PD and incidental Lewy body disease, levels of Cu and Cu transporter protein 1, were significantly reduced in surviving neurons in the SN and LC. Specific activity of the cuproprotein superoxide dismutase 1 was unchanged in the SN in PD but was enhanced in the parkinsonian anterior cingulate cortex, a region with α-synuclein pathology, normal Cu, and limited cell loss. These data suggest that regions affected by α-synuclein pathology may display enhanced vulnerability and cell loss if Cu-dependent protective mechanisms are compromised. Additional investigation of copper pathology in PD may identify novel targets for the development of protective therapies for this disorder.
DOI: 10.1016/j.neurobiolaging.2013.09.034
PubMed: 24176624
Links to Exploration step
pubmed:24176624Le document en format XML
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Electronic address: bohic@esrf.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Carmona, Asunci N" sort="Carmona, Asunci N" uniqKey="Carmona A" first="Asunci N" last="Carmona">Asunci N Carmona</name><affiliation><nlm:affiliation>University of Bordeaux, Centre d'Etudes Nucléaires de Bordeaux Gradignan, Unité Mixte de Recherche 5797, Gradignan, France; Centre National de la Recherche Scientifique, IN2P3, CENBG, UMR 5797, Gradignan, France.</nlm:affiliation></affiliation></author><author><name sortKey="Ortega, Richard" sort="Ortega, Richard" uniqKey="Ortega R" first="Richard" last="Ortega">Richard Ortega</name><affiliation><nlm:affiliation>University of Bordeaux, Centre d'Etudes Nucléaires de Bordeaux Gradignan, Unité Mixte de Recherche 5797, Gradignan, France; Centre National de la Recherche Scientifique, IN2P3, CENBG, UMR 5797, Gradignan, France.</nlm:affiliation></affiliation></author><author><name sortKey="Cottam, Veronica" sort="Cottam, Veronica" uniqKey="Cottam V" first="Veronica" last="Cottam">Veronica Cottam</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Hare, Dominic J" sort="Hare, Dominic J" uniqKey="Hare D" first="Dominic J" last="Hare">Dominic J. 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Mercer</name><affiliation><nlm:affiliation>Centre for Cellular and Molecular Biology, Deakin University, Melbourne, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Double, Kay L" sort="Double, Kay L" uniqKey="Double K" first="Kay L" last="Double">Kay L. Double</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia; Discipline of Biomedical Science, School of Medical Sciences, Sydney Medical School, The University of Sydney, Australia. 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Davies</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Bohic, Sylvain" sort="Bohic, Sylvain" uniqKey="Bohic S" first="Sylvain" last="Bohic">Sylvain Bohic</name><affiliation><nlm:affiliation>Inserm, U836, Team 6, Rayonnement Synchrotron et Recherche Médicales, Grenoble Institut des Neurosciences, Grenoble, France; European Synchrotron Radiation Facility, BP220, Grenoble, France; Université Joseph Fourier 1, Grenoble Institut des Neurosciences, Grenoble, France. Electronic address: bohic@esrf.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Carmona, Asunci N" sort="Carmona, Asunci N" uniqKey="Carmona A" first="Asunci N" last="Carmona">Asunci N Carmona</name><affiliation><nlm:affiliation>University of Bordeaux, Centre d'Etudes Nucléaires de Bordeaux Gradignan, Unité Mixte de Recherche 5797, Gradignan, France; Centre National de la Recherche Scientifique, IN2P3, CENBG, UMR 5797, Gradignan, France.</nlm:affiliation></affiliation></author><author><name sortKey="Ortega, Richard" sort="Ortega, Richard" uniqKey="Ortega R" first="Richard" last="Ortega">Richard Ortega</name><affiliation><nlm:affiliation>University of Bordeaux, Centre d'Etudes Nucléaires de Bordeaux Gradignan, Unité Mixte de Recherche 5797, Gradignan, France; Centre National de la Recherche Scientifique, IN2P3, CENBG, UMR 5797, Gradignan, France.</nlm:affiliation></affiliation></author><author><name sortKey="Cottam, Veronica" sort="Cottam, Veronica" uniqKey="Cottam V" first="Veronica" last="Cottam">Veronica Cottam</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Hare, Dominic J" sort="Hare, Dominic J" uniqKey="Hare D" first="Dominic J" last="Hare">Dominic J. Hare</name><affiliation><nlm:affiliation>Elemental Bio-imaging Facility, University of Technology, Sydney, Australia; The Florey Institute of Neuroscience and Mental Health, University of Melbourne, Parkville, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Finberg, John P M" sort="Finberg, John P M" uniqKey="Finberg J" first="John P M" last="Finberg">John P M. Finberg</name><affiliation><nlm:affiliation>Faculty of Medicine, Technion, Haifa, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="Reyes, Stefanie" sort="Reyes, Stefanie" uniqKey="Reyes S" first="Stefanie" last="Reyes">Stefanie Reyes</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Halliday, Glenda M" sort="Halliday, Glenda M" uniqKey="Halliday G" first="Glenda M" last="Halliday">Glenda M. Halliday</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Mercer, Julian F B" sort="Mercer, Julian F B" uniqKey="Mercer J" first="Julian F B" last="Mercer">Julian F B. Mercer</name><affiliation><nlm:affiliation>Centre for Cellular and Molecular Biology, Deakin University, Melbourne, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Double, Kay L" sort="Double, Kay L" uniqKey="Double K" first="Kay L" last="Double">Kay L. Double</name><affiliation><nlm:affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia; Discipline of Biomedical Science, School of Medical Sciences, Sydney Medical School, The University of Sydney, Australia. Electronic address: kay.double@sydney.edu.au.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Neurobiology of aging</title><idno type="eISSN">1558-1497</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cation Transport Proteins (metabolism)</term><term>Copper (metabolism)</term><term>Gyrus Cinguli (enzymology)</term><term>Humans</term><term>Locus Coeruleus (cytology)</term><term>Locus Coeruleus (metabolism)</term><term>Molecular Targeted Therapy</term><term>Neurons (metabolism)</term><term>Parkinson Disease (drug therapy)</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (metabolism)</term><term>Substantia Nigra (cytology)</term><term>Substantia Nigra (metabolism)</term><term>Superoxide Dismutase (metabolism)</term><term>Superoxide Dismutase-1</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cation Transport Proteins</term><term>Copper</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Locus Coeruleus</term><term>Substantia Nigra</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Gyrus Cinguli</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Locus Coeruleus</term><term>Neurons</term><term>Parkinson Disease</term><term>Substantia Nigra</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Molecular Targeted Therapy</term><term>Superoxide Dismutase-1</term><term>alpha-Synuclein</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Synchrotron-based x-ray fluorescence microscopy, immunofluorescence, and Western blotting were used to investigate changes in copper (Cu) and Cu-associated pathways in the vulnerable substantia nigra (SN) and locus coeruleus (LC) and in nondegenerating brain regions in cases of Parkinson's disease (PD) and appropriate healthy and disease controls. In PD and incidental Lewy body disease, levels of Cu and Cu transporter protein 1, were significantly reduced in surviving neurons in the SN and LC. Specific activity of the cuproprotein superoxide dismutase 1 was unchanged in the SN in PD but was enhanced in the parkinsonian anterior cingulate cortex, a region with α-synuclein pathology, normal Cu, and limited cell loss. These data suggest that regions affected by α-synuclein pathology may display enhanced vulnerability and cell loss if Cu-dependent protective mechanisms are compromised. Additional investigation of copper pathology in PD may identify novel targets for the development of protective therapies for this disorder.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24176624</PMID><DateCreated><Year>2014</Year><Month>01</Month><Day>03</Day></DateCreated><DateCompleted><Year>2014</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1558-1497</ISSN><JournalIssue CitedMedium="Internet"><Volume>35</Volume><Issue>4</Issue><PubDate><Year>2014</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Neurobiology of aging</Title><ISOAbbreviation>Neurobiol. Aging</ISOAbbreviation></Journal><ArticleTitle>Copper pathology in vulnerable brain regions in Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>858-66</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.neurobiolaging.2013.09.034</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0197-4580(13)00436-3</ELocationID><Abstract><AbstractText>Synchrotron-based x-ray fluorescence microscopy, immunofluorescence, and Western blotting were used to investigate changes in copper (Cu) and Cu-associated pathways in the vulnerable substantia nigra (SN) and locus coeruleus (LC) and in nondegenerating brain regions in cases of Parkinson's disease (PD) and appropriate healthy and disease controls. In PD and incidental Lewy body disease, levels of Cu and Cu transporter protein 1, were significantly reduced in surviving neurons in the SN and LC. Specific activity of the cuproprotein superoxide dismutase 1 was unchanged in the SN in PD but was enhanced in the parkinsonian anterior cingulate cortex, a region with α-synuclein pathology, normal Cu, and limited cell loss. These data suggest that regions affected by α-synuclein pathology may display enhanced vulnerability and cell loss if Cu-dependent protective mechanisms are compromised. Additional investigation of copper pathology in PD may identify novel targets for the development of protective therapies for this disorder.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Davies</LastName><ForeName>Katherine M</ForeName><Initials>KM</Initials><AffiliationInfo><Affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bohic</LastName><ForeName>Sylvain</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Inserm, U836, Team 6, Rayonnement Synchrotron et Recherche Médicales, Grenoble Institut des Neurosciences, Grenoble, France; European Synchrotron Radiation Facility, BP220, Grenoble, France; Université Joseph Fourier 1, Grenoble Institut des Neurosciences, Grenoble, France. Electronic address: bohic@esrf.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carmona</LastName><ForeName>Asunción</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>University of Bordeaux, Centre d'Etudes Nucléaires de Bordeaux Gradignan, Unité Mixte de Recherche 5797, Gradignan, France; Centre National de la Recherche Scientifique, IN2P3, CENBG, UMR 5797, Gradignan, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ortega</LastName><ForeName>Richard</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>University of Bordeaux, Centre d'Etudes Nucléaires de Bordeaux Gradignan, Unité Mixte de Recherche 5797, Gradignan, France; Centre National de la Recherche Scientifique, IN2P3, CENBG, UMR 5797, Gradignan, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cottam</LastName><ForeName>Veronica</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Neuroscience Research Australia, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hare</LastName><ForeName>Dominic J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Elemental Bio-imaging Facility, University of Technology, Sydney, Australia; The Florey Institute of Neuroscience and Mental Health, University of Melbourne, Parkville, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Finberg</LastName><ForeName>John P M</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Faculty of Medicine, Technion, Haifa, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reyes</LastName><ForeName>Stefanie</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Halliday</LastName><ForeName>Glenda M</ForeName><Initials>GM</Initials><AffiliationInfo><Affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mercer</LastName><ForeName>Julian F B</ForeName><Initials>JF</Initials><AffiliationInfo><Affiliation>Centre for Cellular and Molecular Biology, Deakin University, Melbourne, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Double</LastName><ForeName>Kay L</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>Neuroscience Research Australia, Sydney, Australia; School of Medical Sciences, Faculty of Medicine, University of New South Wales, Sydney, Australia; Discipline of Biomedical Science, School of Medical Sciences, Sydney Medical School, The University of Sydney, Australia. Electronic address: kay.double@sydney.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R24AA012725</GrantID><Acronym>AA</Acronym><Agency>NIAAA NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>10</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Neurobiol Aging</MedlineTA><NlmUniqueID>8100437</NlmUniqueID><ISSNLinking>0197-4580</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D027682">Cation Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C490079">SLC31A1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000606290">SOD1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.15.1.1</RegistryNumber><NameOfSubstance UI="D013482">Superoxide Dismutase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.15.1.1</RegistryNumber><NameOfSubstance UI="D000072105">Superoxide Dismutase-1</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D027682" MajorTopicYN="N">Cation Transport Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006179" MajorTopicYN="N">Gyrus Cinguli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008125" MajorTopicYN="N">Locus Coeruleus</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058990" MajorTopicYN="N">Molecular Targeted Therapy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013378" MajorTopicYN="N">Substantia Nigra</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013482" MajorTopicYN="N">Superoxide Dismutase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000072105" MajorTopicYN="N">Superoxide Dismutase-1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Copper</Keyword><Keyword MajorTopicYN="N">Copper transporter 1 (Ctr1)</Keyword><Keyword MajorTopicYN="N">Human brain</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">Substantia nigra</Keyword><Keyword MajorTopicYN="N">Superoxide dismutase 1 (SOD1)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>04</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>09</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>09</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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