Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases.
Identifieur interne : 000A62 ( PubMed/Corpus ); précédent : 000A61; suivant : 000A63Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases.
Auteurs : Jacques Fantini ; Nouara YahiSource :
- Expert reviews in molecular medicine [ 1462-3994 ] ; 2010.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Amyloid, Cholesterol, Sphingolipids.
- metabolism : Cell Membrane, Neurodegenerative Diseases.
- Animals, Humans, Models, Biological.
Abstract
Alzheimer, Parkinson and other neurodegenerative diseases involve a series of brain proteins, referred to as 'amyloidogenic proteins', with exceptional conformational plasticity and a high propensity for self-aggregation. Although the mechanisms by which amyloidogenic proteins kill neural cells are not fully understood, a common feature is the concentration of unstructured amyloidogenic monomers on bidimensional membrane lattices. Membrane-bound monomers undergo a series of lipid-dependent conformational changes, leading to the formation of oligomers of varying toxicity rich in beta-sheet structures (annular pores, amyloid fibrils) or in alpha-helix structures (transmembrane channels). Condensed membrane nano- or microdomains formed by sphingolipids and cholesterol are privileged sites for the binding and oligomerisation of amyloidogenic proteins. By controlling the balance between unstructured monomers and alpha or beta conformers (the chaperone effect), sphingolipids can either inhibit or stimulate the oligomerisation of amyloidogenic proteins. Cholesterol has a dual role: regulation of protein-sphingolipid interactions through a fine tuning of sphingolipid conformation (indirect effect), and facilitation of pore (or channel) formation through direct binding to amyloidogenic proteins. Deciphering this complex network of molecular interactions in the context of age- and disease-related evolution of brain lipid expression will help understanding of how amyloidogenic proteins induce neural toxicity and will stimulate the development of innovative therapies for neurodegenerative diseases.
DOI: 10.1017/S1462399410001602
PubMed: 20807455
Links to Exploration step
pubmed:20807455Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases.</title><author><name sortKey="Fantini, Jacques" sort="Fantini, Jacques" uniqKey="Fantini J" first="Jacques" last="Fantini">Jacques Fantini</name><affiliation><nlm:affiliation>Laboratoire des Interactions Moléculaires et Systèmes Membranaires, Marseille, France. jacques.fantini@univ-cezanne.fr</nlm:affiliation></affiliation></author><author><name sortKey="Yahi, Nouara" sort="Yahi, Nouara" uniqKey="Yahi N" first="Nouara" last="Yahi">Nouara Yahi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20807455</idno><idno type="pmid">20807455</idno><idno type="doi">10.1017/S1462399410001602</idno><idno type="wicri:Area/PubMed/Corpus">000A62</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A62</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases.</title><author><name sortKey="Fantini, Jacques" sort="Fantini, Jacques" uniqKey="Fantini J" first="Jacques" last="Fantini">Jacques Fantini</name><affiliation><nlm:affiliation>Laboratoire des Interactions Moléculaires et Systèmes Membranaires, Marseille, France. jacques.fantini@univ-cezanne.fr</nlm:affiliation></affiliation></author><author><name sortKey="Yahi, Nouara" sort="Yahi, Nouara" uniqKey="Yahi N" first="Nouara" last="Yahi">Nouara Yahi</name></author></analytic><series><title level="j">Expert reviews in molecular medicine</title><idno type="eISSN">1462-3994</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid (metabolism)</term><term>Animals</term><term>Cell Membrane (metabolism)</term><term>Cholesterol (metabolism)</term><term>Humans</term><term>Models, Biological</term><term>Neurodegenerative Diseases (metabolism)</term><term>Sphingolipids (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloid</term><term>Cholesterol</term><term>Sphingolipids</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Neurodegenerative Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Models, Biological</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Alzheimer, Parkinson and other neurodegenerative diseases involve a series of brain proteins, referred to as 'amyloidogenic proteins', with exceptional conformational plasticity and a high propensity for self-aggregation. Although the mechanisms by which amyloidogenic proteins kill neural cells are not fully understood, a common feature is the concentration of unstructured amyloidogenic monomers on bidimensional membrane lattices. Membrane-bound monomers undergo a series of lipid-dependent conformational changes, leading to the formation of oligomers of varying toxicity rich in beta-sheet structures (annular pores, amyloid fibrils) or in alpha-helix structures (transmembrane channels). Condensed membrane nano- or microdomains formed by sphingolipids and cholesterol are privileged sites for the binding and oligomerisation of amyloidogenic proteins. By controlling the balance between unstructured monomers and alpha or beta conformers (the chaperone effect), sphingolipids can either inhibit or stimulate the oligomerisation of amyloidogenic proteins. Cholesterol has a dual role: regulation of protein-sphingolipid interactions through a fine tuning of sphingolipid conformation (indirect effect), and facilitation of pore (or channel) formation through direct binding to amyloidogenic proteins. Deciphering this complex network of molecular interactions in the context of age- and disease-related evolution of brain lipid expression will help understanding of how amyloidogenic proteins induce neural toxicity and will stimulate the development of innovative therapies for neurodegenerative diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20807455</PMID><DateCreated><Year>2010</Year><Month>09</Month><Day>02</Day></DateCreated><DateCompleted><Year>2010</Year><Month>09</Month><Day>23</Day></DateCompleted><DateRevised><Year>2014</Year><Month>12</Month><Day>03</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1462-3994</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><PubDate><Year>2010</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Expert reviews in molecular medicine</Title><ISOAbbreviation>Expert Rev Mol Med</ISOAbbreviation></Journal><ArticleTitle>Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases.</ArticleTitle><Pagination><MedlinePgn>e27</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1017/S1462399410001602</ELocationID><Abstract><AbstractText>Alzheimer, Parkinson and other neurodegenerative diseases involve a series of brain proteins, referred to as 'amyloidogenic proteins', with exceptional conformational plasticity and a high propensity for self-aggregation. Although the mechanisms by which amyloidogenic proteins kill neural cells are not fully understood, a common feature is the concentration of unstructured amyloidogenic monomers on bidimensional membrane lattices. Membrane-bound monomers undergo a series of lipid-dependent conformational changes, leading to the formation of oligomers of varying toxicity rich in beta-sheet structures (annular pores, amyloid fibrils) or in alpha-helix structures (transmembrane channels). Condensed membrane nano- or microdomains formed by sphingolipids and cholesterol are privileged sites for the binding and oligomerisation of amyloidogenic proteins. By controlling the balance between unstructured monomers and alpha or beta conformers (the chaperone effect), sphingolipids can either inhibit or stimulate the oligomerisation of amyloidogenic proteins. Cholesterol has a dual role: regulation of protein-sphingolipid interactions through a fine tuning of sphingolipid conformation (indirect effect), and facilitation of pore (or channel) formation through direct binding to amyloidogenic proteins. Deciphering this complex network of molecular interactions in the context of age- and disease-related evolution of brain lipid expression will help understanding of how amyloidogenic proteins induce neural toxicity and will stimulate the development of innovative therapies for neurodegenerative diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fantini</LastName><ForeName>Jacques</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Laboratoire des Interactions Moléculaires et Systèmes Membranaires, Marseille, France. jacques.fantini@univ-cezanne.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yahi</LastName><ForeName>Nouara</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>09</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Expert Rev Mol Med</MedlineTA><NlmUniqueID>100939725</NlmUniqueID><ISSNLinking>1462-3994</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000682">Amyloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013107">Sphingolipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>97C5T2UQ7J</RegistryNumber><NameOfSubstance UI="D002784">Cholesterol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>BMC Genomics. 2009;10 Suppl 1:S7</RefSource><PMID Version="1">19594884</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Neurol Sci. 2009 Aug 15;283(1-2):230-4</RefSource><PMID 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019636" MajorTopicYN="N">Neurodegenerative Diseases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013107" MajorTopicYN="N">Sphingolipids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>150</NumberOfReferences><OtherID Source="NLM">PMC2931503</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>9</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>9</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>9</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20807455</ArticleId><ArticleId IdType="pii">S1462399410001602</ArticleId><ArticleId IdType="doi">10.1017/S1462399410001602</ArticleId><ArticleId IdType="pmc">PMC2931503</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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