In:
Journal of Biomedicine and Biotechnology, Hindawi Limited, Vol. 2012 ( 2012), p. 1-7
Abstract:
Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression of α-synuclein, underlie neurodegenerative diseases including Alzheimer’s, Parkinson, Huntington, Creutzfeldt diseases. Small heat-shock proteins, such as αB-crystallin, act as chaperones to prevent protein aggregation and play a key role in the prevention of such protein disorganisation diseases. In this study, we have explored the potential for chaperone activity of αB-crystallin to suppress the formation of protein aggregates. We tested the ability of αB-crystallin to suppress the aggregation of a polyQ protein and α-synuclein in Drosophila . We found that αB-crystallin suppresses both the compound eye degeneration induced by polyQ and the α-synuclein-induced rough eye phenotype. Furthermore, by using histochemical staining we have determined that αB-crystallin inhibits the aggregation of polyQ in vivo . These data provide a clue for the development of therapeutics for neurodegenerative diseases.
Type of Medium:
Online Resource
ISSN:
1110-7243
,
1110-7251
Language:
English
Publisher:
Hindawi Limited
Publication Date:
2012
detail.hit.zdb_id:
2698540-8
detail.hit.zdb_id:
2512507-2
SSG:
12
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