You are here: Home :: Area NEM :: Life sciences :: Biochemistry

Erich E. Wanker

Protein Aggregation and Pathogenesis of Huntingtons Disease: Mechanisms and Correlations

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.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 381, 09/2000
Pages: 937 - 942

Show full article (external site)

Show all available items of this journal

 

Area NEM