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rdf:type |
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lifeskim:mentions |
umls-concept:C0006104,
umls-concept:C0017262,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0086418,
umls-concept:C0185027,
umls-concept:C0185117,
umls-concept:C0376315,
umls-concept:C0449774,
umls-concept:C0871261,
umls-concept:C1167059,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911684,
umls-concept:C2911692
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pubmed:issue |
2
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pubmed:dateCreated |
2005-10-24
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pubmed:abstractText |
Lewy bodies (LBs) are the characteristic inclusions of Parkinson's disease brain but the mechanism responsible for their formation is obscure. Lewy bodies (LBs) are composed of a number of proteins of which alpha-synuclein (alpha-SYN) is a major constituent. In this study, we have investigated the distribution patterns of synphilin-1 and parkin proteins in control and sporadic PD brain tissue by immunohistochemistry (IH), immunoblotting, and immunoelectron microscopy (IEM). We demonstrate the presence of synphilin-1 and parkin in the central core of a majority of LBs using IH and IEM. Using IH, we show an overlapping distribution profile of the two proteins in central neurons. Additionally, we show sensitivity of both endogenous synphilin-1 and parkin to proteolytic dysfunction and their co-localization in aggresomes formed in response to the proteasome inhibitor MG-132. We confirm that synphilin-1 and parkin are components of majority of LBs in Parkinson's disease and that both proteins are susceptible to proteasomal degradation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0969-9961
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pubmed:author |
pubmed-author:BandopadhyayRinaR,
pubmed-author:EngelenderSimoneS,
pubmed-author:HarveyKirstenK,
pubmed-author:HarveyRobert JRJ,
pubmed-author:KilfordLindaL,
pubmed-author:KingsburyAnn EAE,
pubmed-author:LatchmanDavid SDS,
pubmed-author:LeesAndrew JAJ,
pubmed-author:MuqitMiratul MMM,
pubmed-author:ReidAndrew RAR,
pubmed-author:SchlossmacherMichael GMG,
pubmed-author:WoodNicholas WNW
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
401-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15894486-Aged,
pubmed-meshheading:15894486-Aged, 80 and over,
pubmed-meshheading:15894486-Brain,
pubmed-meshheading:15894486-Carrier Proteins,
pubmed-meshheading:15894486-Cell Line, Tumor,
pubmed-meshheading:15894486-Cerebral Cortex,
pubmed-meshheading:15894486-Enzyme Inhibitors,
pubmed-meshheading:15894486-Female,
pubmed-meshheading:15894486-Humans,
pubmed-meshheading:15894486-Immunohistochemistry,
pubmed-meshheading:15894486-Lewy Bodies,
pubmed-meshheading:15894486-Male,
pubmed-meshheading:15894486-Microscopy, Electron, Transmission,
pubmed-meshheading:15894486-Middle Aged,
pubmed-meshheading:15894486-Nerve Tissue Proteins,
pubmed-meshheading:15894486-Neurons,
pubmed-meshheading:15894486-Parkinson Disease,
pubmed-meshheading:15894486-Peptide Hydrolases,
pubmed-meshheading:15894486-Proteasome Endopeptidase Complex,
pubmed-meshheading:15894486-Substantia Nigra,
pubmed-meshheading:15894486-Ubiquitin-Protein Ligases
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pubmed:year |
2005
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pubmed:articleTitle |
Synphilin-1 and parkin show overlapping expression patterns in human brain and form aggresomes in response to proteasomal inhibition.
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pubmed:affiliation |
Reta Lila Weston Institute of Neurological Studies, Royal Free and UCL Medical School, The Windeyer Building, 46 Cleveland Street, London W1T 4JF, UK. regtrib@ucl.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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