α-Synuclein and Lewy pathology in Parkinson's disease.
Identifieur interne : 000445 ( PubMed/Corpus ); précédent : 000444; suivant : 000446α-Synuclein and Lewy pathology in Parkinson's disease.
Auteurs : Lorraine V. Kalia ; Suneil K. KaliaSource :
- Current opinion in neurology [ 1473-6551 ] ; 2015.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : alpha-Synuclein.
- metabolism : Brain, Neurons, Parkinson Disease.
- pathology : Brain, Lewy Bodies, Neurons, Parkinson Disease.
- Humans.
Abstract
The role of protein aggregates, such as Lewy body inclusions, in the molecular pathogenesis of Parkinson's disease has remained controversial and elusive. The protein α-synuclein is a major component of these inclusions but it can exist in many alternate conformations. Here we review advances in our understanding of the roles of Lewy pathology and α-synuclein in Parkinson's disease.
DOI: 10.1097/WCO.0000000000000215
PubMed: 26110807
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Kalia</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26110807</idno><idno type="pmid">26110807</idno><idno type="doi">10.1097/WCO.0000000000000215</idno><idno type="wicri:Area/PubMed/Corpus">000445</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000445</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">α-Synuclein and Lewy pathology in Parkinson's disease.</title><author><name sortKey="Kalia, Lorraine V" sort="Kalia, Lorraine V" uniqKey="Kalia L" first="Lorraine V" last="Kalia">Lorraine V. Kalia</name><affiliation><nlm:affiliation>aDivision of Neurology, Department of Medicine bDivision of Neurosurgery, Department of Surgery cTanz Centre for Research in Neurodegenerative Diseases, University of Toronto dMorton and Gloria Shulman Movement Disorders Clinic and the Edmond J. Safra Program in Parkinson's Disease, Division of Neurology, Department of Medicine eToronto Western Research Institute, Toronto Western Hospital, University Health Network, Toronto, ON, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Kalia, Suneil K" sort="Kalia, Suneil K" uniqKey="Kalia S" first="Suneil K" last="Kalia">Suneil K. Kalia</name></author></analytic><series><title level="j">Current opinion in neurology</title><idno type="eISSN">1473-6551</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Brain (metabolism)</term><term>Brain (pathology)</term><term>Humans</term><term>Lewy Bodies (pathology)</term><term>Neurons (metabolism)</term><term>Neurons (pathology)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (pathology)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term><term>Neurons</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Brain</term><term>Lewy Bodies</term><term>Neurons</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The role of protein aggregates, such as Lewy body inclusions, in the molecular pathogenesis of Parkinson's disease has remained controversial and elusive. The protein α-synuclein is a major component of these inclusions but it can exist in many alternate conformations. Here we review advances in our understanding of the roles of Lewy pathology and α-synuclein in Parkinson's disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26110807</PMID><DateCreated><Year>2015</Year><Month>07</Month><Day>03</Day></DateCreated><DateCompleted><Year>2016</Year><Month>04</Month><Day>06</Day></DateCompleted><DateRevised><Year>2015</Year><Month>07</Month><Day>03</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1473-6551</ISSN><JournalIssue CitedMedium="Internet"><Volume>28</Volume><Issue>4</Issue><PubDate><Year>2015</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Current opinion in neurology</Title><ISOAbbreviation>Curr. Opin. Neurol.</ISOAbbreviation></Journal><ArticleTitle>α-Synuclein and Lewy pathology in Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>375-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1097/WCO.0000000000000215</ELocationID><Abstract><AbstractText Label="PURPOSE OF REVIEW" NlmCategory="OBJECTIVE">The role of protein aggregates, such as Lewy body inclusions, in the molecular pathogenesis of Parkinson's disease has remained controversial and elusive. The protein α-synuclein is a major component of these inclusions but it can exist in many alternate conformations. Here we review advances in our understanding of the roles of Lewy pathology and α-synuclein in Parkinson's disease.</AbstractText><AbstractText Label="RECENT FINDINGS" NlmCategory="RESULTS">Recent work has demonstrated that certain α-synuclein conformations are directly toxic to neurons and may also propagate Lewy pathology within the nervous system. Investigation into clinicopathological correlates in rare genetic forms of Parkinson's disease has revealed that Lewy pathology is associated with nonmotor features but may not contribute to motor symptoms in Parkinson's disease.</AbstractText><AbstractText Label="SUMMARY" NlmCategory="CONCLUSIONS">These recent findings open up new avenues of investigation into the molecular pathogenesis of Parkinson's disease. Future work will need to identify the most toxic conformations of α-synuclein and define their relationship to Lewy pathology. This work will be necessary to be able to develop novel therapeutic strategies that target specific pathogenic forms of α-synuclein for disease modification in Parkinson's disease.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kalia</LastName><ForeName>Lorraine V</ForeName><Initials>LV</Initials><AffiliationInfo><Affiliation>aDivision of Neurology, Department of Medicine bDivision of Neurosurgery, Department of Surgery cTanz Centre for Research in Neurodegenerative Diseases, University of Toronto dMorton and Gloria Shulman Movement Disorders Clinic and the Edmond J. Safra Program in Parkinson's Disease, Division of Neurology, Department of Medicine eToronto Western Research Institute, Toronto Western Hospital, University Health Network, Toronto, ON, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kalia</LastName><ForeName>Suneil K</ForeName><Initials>SK</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Curr Opin Neurol</MedlineTA><NlmUniqueID>9319162</NlmUniqueID><ISSNLinking>1350-7540</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016631" MajorTopicYN="N">Lewy Bodies</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>4</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26110807</ArticleId><ArticleId IdType="doi">10.1097/WCO.0000000000000215</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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