Neuropathology of synuclein aggregates
Identifieur interne : 002F70 ( Main/Corpus ); précédent : 002F69; suivant : 002F71Neuropathology of synuclein aggregates
Auteurs : John E. Duda ; Virginia M. Lee ; John Q. TrojanowskiSource :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2000-07-15.
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Abstract
Beginning with the isolation of the fragment of α‐synuclein (α‐syn) known as the non‐Aβ component of amyloid plaques (NAC peptide) from Alzheimer's disease (AD) brains, α‐syn has been increasingly implicated in the pathogenesis of neurodegenerative diseases, which now are classified as synucleinopathies. Indeed, unequivocal evidence linking abnormal α‐syn to mechanisms of brain degeneration came from discoveries of missense mutations in the α‐syn gene pathogenic for familial Parkinson's disease (PD) in rare kindreds. Shortly thereafter, α‐syn was shown to be a major component of Lewy bodies (LBs) and Lewy neurites in sporadic PD, dementia with LBs (DLB) and the LB variant of AD. Also, studies of brains from patients with AD caused by genetic abnormalities demonstrated many α‐syn positive LBs. Further, α‐syn was implicated in the formation of the glial (GCIs) and neuronal cytoplasmic inclusions of multiple system atrophy, and the LBs, GCIs and neuraxonal spheroids of neurodegeneration with brain iron accumulation type 1. Recently, two other members of the synuclein family, β‐ and γ‐synuclein, have also been recognized to play a role in the pathogenesis of novel axonal lesions in PD and DLB. Evidence for a role of α‐syn in the formation of filamentous aggregates was reinforced by in vitro studies showing aggregation and fibrillogenesis of mutant and wild type α‐syn. Indeed, since the aggregation of brain proteins into presumptively toxic lesions is emerging as a common but poorly understood mechanistic theme in sporadic and hereditary neurodegenerative diseases, clarification of the mechanism of synuclein aggregation could augment efforts to develop novel and more effective therapies for many neurodegenerative disorders. J. Neurosci. Res. 61:121–127, 2000. © 2000 Wiley‐Liss, Inc.
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DOI: 10.1002/1097-4547(20000715)61:2<121::AID-JNR1>3.0.CO;2-4
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Indeed, unequivocal evidence linking abnormal α‐syn to mechanisms of brain degeneration came from discoveries of missense mutations in the α‐syn gene pathogenic for familial Parkinson's disease (PD) in rare kindreds. Shortly thereafter, α‐syn was shown to be a major component of Lewy bodies (LBs) and Lewy neurites in sporadic PD, dementia with LBs (DLB) and the LB variant of AD. Also, studies of brains from patients with AD caused by genetic abnormalities demonstrated many α‐syn positive LBs. Further, α‐syn was implicated in the formation of the glial (GCIs) and neuronal cytoplasmic inclusions of multiple system atrophy, and the LBs, GCIs and neuraxonal spheroids of neurodegeneration with brain iron accumulation type 1. Recently, two other members of the synuclein family, β‐ and γ‐synuclein, have also been recognized to play a role in the pathogenesis of novel axonal lesions in PD and DLB. Evidence for a role of α‐syn in the formation of filamentous aggregates was reinforced by in vitro studies showing aggregation and fibrillogenesis of mutant and wild type α‐syn. Indeed, since the aggregation of brain proteins into presumptively toxic lesions is emerging as a common but poorly understood mechanistic theme in sporadic and hereditary neurodegenerative diseases, clarification of the mechanism of synuclein aggregation could augment efforts to develop novel and more effective therapies for many neurodegenerative disorders. J. Neurosci. Res. 61:121–127, 2000. © 2000 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>John E. Duda</name><affiliations><json:string>Center For Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia</json:string></affiliations></json:item><json:item><name>Virginia M.‐Y. Lee</name><affiliations><json:string>Center For Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia</json:string></affiliations></json:item><json:item><name>John Q. Trojanowski</name><affiliations><json:string>Center For Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>α‐synuclein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Alzheimer's disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Parkinson's disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>multiple system atrophy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>dementia with Lewy bodies</value></json:item></subject><articleId><json:string>JNR1</json:string></articleId><language><json:string>eng</json:string></language><abstract>Beginning with the isolation of the fragment of α‐synuclein (α‐syn) known as the non‐Aβ component of amyloid plaques (NAC peptide) from Alzheimer's disease (AD) brains, α‐syn has been increasingly implicated in the pathogenesis of neurodegenerative diseases, which now are classified as synucleinopathies. Indeed, unequivocal evidence linking abnormal α‐syn to mechanisms of brain degeneration came from discoveries of missense mutations in the α‐syn gene pathogenic for familial Parkinson's disease (PD) in rare kindreds. Shortly thereafter, α‐syn was shown to be a major component of Lewy bodies (LBs) and Lewy neurites in sporadic PD, dementia with LBs (DLB) and the LB variant of AD. Also, studies of brains from patients with AD caused by genetic abnormalities demonstrated many α‐syn positive LBs. Further, α‐syn was implicated in the formation of the glial (GCIs) and neuronal cytoplasmic inclusions of multiple system atrophy, and the LBs, GCIs and neuraxonal spheroids of neurodegeneration with brain iron accumulation type 1. Recently, two other members of the synuclein family, β‐ and γ‐synuclein, have also been recognized to play a role in the pathogenesis of novel axonal lesions in PD and DLB. Evidence for a role of α‐syn in the formation of filamentous aggregates was reinforced by in vitro studies showing aggregation and fibrillogenesis of mutant and wild type α‐syn. Indeed, since the aggregation of brain proteins into presumptively toxic lesions is emerging as a common but poorly understood mechanistic theme in sporadic and hereditary neurodegenerative diseases, clarification of the mechanism of synuclein aggregation could augment efforts to develop novel and more effective therapies for many neurodegenerative disorders. J. Neurosci. 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Indeed, unequivocal evidence linking abnormal α‐syn to mechanisms of brain degeneration came from discoveries of missense mutations in the α‐syn gene pathogenic for familial Parkinson's disease (PD) in rare kindreds. Shortly thereafter, α‐syn was shown to be a major component of Lewy bodies (LBs) and Lewy neurites in sporadic PD, dementia with LBs (DLB) and the LB variant of AD. Also, studies of brains from patients with AD caused by genetic abnormalities demonstrated many α‐syn positive LBs. Further, α‐syn was implicated in the formation of the glial (GCIs) and neuronal cytoplasmic inclusions of multiple system atrophy, and the LBs, GCIs and neuraxonal spheroids of neurodegeneration with brain iron accumulation type 1. Recently, two other members of the synuclein family, β‐ and γ‐synuclein, have also been recognized to play a role in the pathogenesis of novel axonal lesions in PD and DLB. Evidence for a role of α‐syn in the formation of filamentous aggregates was reinforced by in vitro studies showing aggregation and fibrillogenesis of mutant and wild type α‐syn. Indeed, since the aggregation of brain proteins into presumptively toxic lesions is emerging as a common but poorly understood mechanistic theme in sporadic and hereditary neurodegenerative diseases, clarification of the mechanism of synuclein aggregation could augment efforts to develop novel and more effective therapies for many neurodegenerative disorders. J. Neurosci. 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Indeed, unequivocal evidence linking abnormal α‐syn to mechanisms of brain degeneration came from discoveries of missense mutations in the α‐syn gene pathogenic for familial Parkinson's disease (PD) in rare kindreds. Shortly thereafter, α‐syn was shown to be a major component of Lewy bodies (LBs) and Lewy neurites in sporadic PD, dementia with LBs (DLB) and the LB variant of AD. Also, studies of brains from patients with AD caused by genetic abnormalities demonstrated many α‐syn positive LBs. Further, α‐syn was implicated in the formation of the glial (GCIs) and neuronal cytoplasmic inclusions of multiple system atrophy, and the LBs, GCIs and neuraxonal spheroids of neurodegeneration with brain iron accumulation type 1. Recently, two other members of the synuclein family, β‐ and γ‐synuclein, have also been recognized to play a role in the pathogenesis of novel axonal lesions in PD and DLB. Evidence for a role of α‐syn in the formation of filamentous aggregates was reinforced by in vitro studies showing aggregation and fibrillogenesis of mutant and wild type α‐syn. Indeed, since the aggregation of brain proteins into presumptively toxic lesions is emerging as a common but poorly understood mechanistic theme in sporadic and hereditary neurodegenerative diseases, clarification of the mechanism of synuclein aggregation could augment efforts to develop novel and more effective therapies for many neurodegenerative disorders. J. Neurosci. Res. 61:121–127, 2000. © 2000 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Neuropathology of synuclein aggregates</title><subTitle>New insights into mechanisms of neurodegenerative diseases</subTitle></titleInfo><titleInfo type="abbreviated" lang="en"><title>Neuropathology of Synucleins</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Neuropathology of synuclein aggregates</title></titleInfo><name type="personal"><namePart type="given">John E.</namePart><namePart type="family">Duda</namePart><affiliation>Center For Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Virginia M.‐Y.</namePart><namePart type="family">Lee</namePart><affiliation>Center For Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John Q.</namePart><namePart type="family">Trojanowski</namePart><affiliation>Center For Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia</affiliation><description>Correspondence: Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, 3rd Floor Maloney Building, Philadelphia, PA 19104</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle"></genre><originInfo><publisher>John Wiley & Sons, Inc.</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2000-07-15</dateIssued><dateCaptured encoding="w3cdtf">2000-02-08</dateCaptured><dateValid encoding="w3cdtf">2000-03-10</dateValid><copyrightDate encoding="w3cdtf">2000</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">3</extent><extent unit="references">52</extent><extent unit="words">5286</extent></physicalDescription><abstract lang="en">Beginning with the isolation of the fragment of α‐synuclein (α‐syn) known as the non‐Aβ component of amyloid plaques (NAC peptide) from Alzheimer's disease (AD) brains, α‐syn has been increasingly implicated in the pathogenesis of neurodegenerative diseases, which now are classified as synucleinopathies. Indeed, unequivocal evidence linking abnormal α‐syn to mechanisms of brain degeneration came from discoveries of missense mutations in the α‐syn gene pathogenic for familial Parkinson's disease (PD) in rare kindreds. Shortly thereafter, α‐syn was shown to be a major component of Lewy bodies (LBs) and Lewy neurites in sporadic PD, dementia with LBs (DLB) and the LB variant of AD. Also, studies of brains from patients with AD caused by genetic abnormalities demonstrated many α‐syn positive LBs. Further, α‐syn was implicated in the formation of the glial (GCIs) and neuronal cytoplasmic inclusions of multiple system atrophy, and the LBs, GCIs and neuraxonal spheroids of neurodegeneration with brain iron accumulation type 1. Recently, two other members of the synuclein family, β‐ and γ‐synuclein, have also been recognized to play a role in the pathogenesis of novel axonal lesions in PD and DLB. Evidence for a role of α‐syn in the formation of filamentous aggregates was reinforced by in vitro studies showing aggregation and fibrillogenesis of mutant and wild type α‐syn. Indeed, since the aggregation of brain proteins into presumptively toxic lesions is emerging as a common but poorly understood mechanistic theme in sporadic and hereditary neurodegenerative diseases, clarification of the mechanism of synuclein aggregation could augment efforts to develop novel and more effective therapies for many neurodegenerative disorders. J. Neurosci. Res. 61:121–127, 2000. © 2000 Wiley‐Liss, Inc.</abstract><note type="funding">National Institute on Aging of the National Institutes of Health</note><note type="funding">Alzheimer's Foundation</note><subject lang="en"><genre>Keywords</genre><topic>α‐synuclein</topic><topic>Alzheimer's disease</topic><topic>Parkinson's disease</topic><topic>multiple system atrophy</topic><topic>dementia with Lewy bodies</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Neuroscience Research</title></titleInfo><titleInfo type="abbreviated"><title>J. Neurosci. Res.</title></titleInfo><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Mini‐Review</topic></subject><identifier type="ISSN">0360-4012</identifier><identifier type="eISSN">1097-4547</identifier><identifier type="DOI">10.1002/(ISSN)1097-4547</identifier><identifier type="PublisherID">JNR</identifier><part><date>2000</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>121</start><end>127</end><total>7</total></extent></part></relatedItem><identifier type="istex">015F38C570E539F91C94D0C21F4ECDD5D777A9BB</identifier><identifier type="DOI">10.1002/1097-4547(20000715)61:2<121::AID-JNR1>3.0.CO;2-4</identifier><identifier type="ArticleID">JNR1</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2000 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>John Wiley & Sons, Inc.</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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