Effect of αB-Crystallin on Protein Aggregation in Drosophila. (11th January 2012)

• Record Type: Journal Article
• Authors: Tue, Nguyen Trong; Shimaji, Kouhei; Tanaka, Naoki; Yamaguchi, Masamitsu
• Other Names: Perry George Academic Editor.
• Is Part Of: Journal of biomedicine and biotechnology. Volume 2012(2012)
• Publication Date: 2012-01-11
• Subjects: Medicine -- Periodicals; Biology -- Periodicals; Biotechnology -- Periodicals; Medicine; Biology; Biotechnology; Médecine; Biologie; Biotechnologie; Biology; Biotechnology; Medicine; Biotechnology; Biomedicine; Electronic journals; Periodical; Periodicals; Electronic journals; 610
• DOI: 10.1155/2012/252049
• Languages: English
• ISSNs: 1110-7243

Abstract

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 α B-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 α B-crystallin to suppress the formation of protein aggregates. We tested the ability of α B-crystallin to suppress the aggregation of a polyQ protein and α -synuclein in Drosophila . We found that α B-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 α B-crystallin inhibits the aggregation of polyQ in vivo . These data provide a clue for the development of therapeutics for neurodegenerative diseases.