Glycosaminoglycans, protein aggregation and neurodegeneration.
Identifieur interne : 000908 ( PubMed/Checkpoint ); précédent : 000907; suivant : 000909Glycosaminoglycans, protein aggregation and neurodegeneration.
Auteurs : Dulce Papy-Garcia [France] ; Morin Christophe ; Minh Bao Huynh ; Sineriz Fernando ; Sissoeff Ludmilla ; Julia Elisa Sepulveda-Diaz ; Rita Raisman-VozariSource :
- Current protein & peptide science [ 1875-5550 ] ; 2011.
English descriptors
- KwdEn :
- Amyloid beta-Peptides (chemistry), Amyloid beta-Peptides (metabolism), Glycosaminoglycans (chemistry), Glycosaminoglycans (metabolism), Humans, Membrane Proteins (chemistry), Membrane Proteins (metabolism), Neurodegenerative Diseases (immunology), Neurodegenerative Diseases (physiopathology), Peptide Fragments (chemistry), Peptide Fragments (metabolism), Prion Diseases, Prions (chemistry), Prions (metabolism), Protein Conformation, Proteins (chemistry), alpha-Synuclein (chemistry), alpha-Synuclein (metabolism).
- MESH :
- chemical , chemistry : Amyloid beta-Peptides, Glycosaminoglycans, Membrane Proteins, Peptide Fragments, Prions, Proteins, alpha-Synuclein.
- chemical , metabolism : Amyloid beta-Peptides, Glycosaminoglycans, Membrane Proteins, Peptide Fragments, Prions, alpha-Synuclein.
- immunology : Neurodegenerative Diseases.
- physiopathology : Neurodegenerative Diseases.
- Humans, Prion Diseases, Protein Conformation.
Abstract
A number of neurodegenerative diseases, as Parkinson, prion, and Alzheimer's diseases, has been directly associated with altered conformations of certain peptides or proteins that assemble to form highly organized aggregates, also called amyloid fibers. Glycosaminoglycans have shown to play important roles on fibrils formation, stability and resistance to proteolysis. This manuscript reviews from basic concepts on the biochemistry and biology of glycosaminoglycans to their implications in neurodegeneration with particular emphasis in pathologic protein aggregation. Prion protein, Aβ42, Tau, and α-synuclein, are all proteins that can interact with glycosaminoglycans. We document here how these interactions may modify protein conformation, aggregation kinetics, and fibers stabilization with important consequences in disease. We also raise questions which answers may make advance the understanding of the implication of GAGs in neurodegeneration.
PubMed: 21348835
Affiliations:
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pubmed:21348835Le document en format XML
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sortKey="Ludmilla, Sissoeff" sort="Ludmilla, Sissoeff" uniqKey="Ludmilla S" first="Sissoeff" last="Ludmilla">Sissoeff Ludmilla</name></author><author><name sortKey="Sepulveda Diaz, Julia Elisa" sort="Sepulveda Diaz, Julia Elisa" uniqKey="Sepulveda Diaz J" first="Julia Elisa" last="Sepulveda-Diaz">Julia Elisa Sepulveda-Diaz</name></author><author><name sortKey="Raisman Vozari, Rita" sort="Raisman Vozari, Rita" uniqKey="Raisman Vozari R" first="Rita" last="Raisman-Vozari">Rita Raisman-Vozari</name></author></analytic><series><title level="j">Current protein & peptide science</title><idno type="eISSN">1875-5550</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid beta-Peptides (chemistry)</term><term>Amyloid beta-Peptides (metabolism)</term><term>Glycosaminoglycans (chemistry)</term><term>Glycosaminoglycans (metabolism)</term><term>Humans</term><term>Membrane Proteins (chemistry)</term><term>Membrane Proteins (metabolism)</term><term>Neurodegenerative Diseases (immunology)</term><term>Neurodegenerative Diseases (physiopathology)</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (metabolism)</term><term>Prion Diseases</term><term>Prions (chemistry)</term><term>Prions (metabolism)</term><term>Protein Conformation</term><term>Proteins (chemistry)</term><term>alpha-Synuclein (chemistry)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Glycosaminoglycans</term><term>Membrane Proteins</term><term>Peptide Fragments</term><term>Prions</term><term>Proteins</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Glycosaminoglycans</term><term>Membrane Proteins</term><term>Peptide Fragments</term><term>Prions</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Neurodegenerative Diseases</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Neurodegenerative Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Prion Diseases</term><term>Protein Conformation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A number of neurodegenerative diseases, as Parkinson, prion, and Alzheimer's diseases, has been directly associated with altered conformations of certain peptides or proteins that assemble to form highly organized aggregates, also called amyloid fibers. Glycosaminoglycans have shown to play important roles on fibrils formation, stability and resistance to proteolysis. This manuscript reviews from basic concepts on the biochemistry and biology of glycosaminoglycans to their implications in neurodegeneration with particular emphasis in pathologic protein aggregation. Prion protein, Aβ42, Tau, and α-synuclein, are all proteins that can interact with glycosaminoglycans. We document here how these interactions may modify protein conformation, aggregation kinetics, and fibers stabilization with important consequences in disease. We also raise questions which answers may make advance the understanding of the implication of GAGs in neurodegeneration.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21348835</PMID><DateCreated><Year>2011</Year><Month>05</Month><Day>11</Day></DateCreated><DateCompleted><Year>2011</Year><Month>08</Month><Day>29</Day></DateCompleted><DateRevised><Year>2012</Year><Month>01</Month><Day>31</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1875-5550</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>3</Issue><PubDate><Year>2011</Year><Month>May</Month></PubDate></JournalIssue><Title>Current protein & peptide science</Title><ISOAbbreviation>Curr. Protein Pept. 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We document here how these interactions may modify protein conformation, aggregation kinetics, and fibers stabilization with important consequences in disease. We also raise questions which answers may make advance the understanding of the implication of GAGs in neurodegeneration.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Papy-Garcia</LastName><ForeName>Dulce</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Laboratoire CRRET, EAC/CNRS, Université Paris Est Créteil Val de Marne, Faculté des Sciences et Technologie, France. papy@u-pec.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Christophe</LastName><ForeName>Morin</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Huynh</LastName><ForeName>Minh Bao</ForeName><Initials>MB</Initials></Author><Author ValidYN="Y"><LastName>Fernando</LastName><ForeName>Sineriz</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Ludmilla</LastName><ForeName>Sissoeff</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Sepulveda-Diaz</LastName><ForeName>Julia Elisa</ForeName><Initials>JE</Initials></Author><Author ValidYN="Y"><LastName>Raisman-Vozari</LastName><ForeName>Rita</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Curr Protein Pept Sci</MedlineTA><NlmUniqueID>100960529</NlmUniqueID><ISSNLinking>1389-2037</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016229">Amyloid beta-Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006025">Glycosaminoglycans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C075222">amyloid beta-protein (1-42)</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C404785">tau 40 protein, human</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016229" MajorTopicYN="N">Amyloid beta-Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017096" MajorTopicYN="N">Prion Diseases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011328" MajorTopicYN="N">Prions</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>01</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>02</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>2</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>2</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>8</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21348835</ArticleId><ArticleId IdType="pii">CPPS-112</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Créteil</li></settlement><orgName><li>Université Paris-Est Créteil Val-de-Marne</li></orgName></list><tree><noCountry><name sortKey="Christophe, Morin" sort="Christophe, Morin" uniqKey="Christophe M" first="Morin" last="Christophe">Morin Christophe</name><name sortKey="Fernando, Sineriz" sort="Fernando, Sineriz" uniqKey="Fernando S" first="Sineriz" last="Fernando">Sineriz Fernando</name><name sortKey="Huynh, Minh Bao" sort="Huynh, Minh Bao" uniqKey="Huynh M" first="Minh Bao" last="Huynh">Minh Bao Huynh</name><name sortKey="Ludmilla, Sissoeff" sort="Ludmilla, Sissoeff" uniqKey="Ludmilla S" first="Sissoeff" last="Ludmilla">Sissoeff Ludmilla</name><name sortKey="Raisman Vozari, Rita" sort="Raisman Vozari, Rita" uniqKey="Raisman Vozari R" first="Rita" last="Raisman-Vozari">Rita Raisman-Vozari</name><name sortKey="Sepulveda Diaz, Julia Elisa" sort="Sepulveda Diaz, Julia Elisa" uniqKey="Sepulveda Diaz J" first="Julia Elisa" last="Sepulveda-Diaz">Julia Elisa Sepulveda-Diaz</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Papy Garcia, Dulce" sort="Papy Garcia, Dulce" uniqKey="Papy Garcia D" first="Dulce" last="Papy-Garcia">Dulce Papy-Garcia</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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