Document Detail

Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations.
MedLine Citation:
PMID:  11076024     Owner:  NLM     Status:  MEDLINE    
The formation of insoluble protein aggregates is a hallmark of Huntington's disease (HD) and related neurodegenerative disorders, such as dentatorubral pallidoluysian atrophy (DRPLA), spinal bulbar muscular atrophy (SBMA) and the spinocerebellar ataxia (SCA) type 1, 2, 3, 6 and 7. These disorders are caused by an expanded polyglutamine (polyQ) tract in otherwise unrelated proteins. They are characterized by late-onset, selective neuropathology, a pathogenic polyQ threshold and a relationship between polyQ length and disease progression. Thus, molecular models of HD and related glutamine-repeat disorders must account for these characteristic features. During the last three years, considerable effort has been invested in the development of in vitro and in vivo model systems to study the mechanisms of protein aggregation in glutamine-repeat disorders and its potential effects on disease progression and neurodegeneration. A selection of these studies is reviewed here. Furthermore, the correlation between aggregate formation and development of HD is discussed.
E E Wanker
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Biological chemistry     Volume:  381     ISSN:  1431-6730     ISO Abbreviation:  Biol. Chem.     Publication Date:    2000 Sep-Oct
Date Detail:
Created Date:  2001-03-06     Completed Date:  2001-06-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9700112     Medline TA:  Biol Chem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  937-42     Citation Subset:  IM    
Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.
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MeSH Terms
Huntington Disease / metabolism*,  pathology
Nerve Tissue Proteins / chemistry,  metabolism*
Reg. No./Substance:
0/Nerve Tissue Proteins

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