Effect of αb-crystallin on protein aggregation in drosophila

Abstract

Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression of -synuclein, underlie neurodegenerative diseases including Alzheimer's, Parkinson, Huntington, Creutzfeldt diseases. Small heat-shock proteins, such as 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 B-crystallin to suppress the formation of protein aggregates. We tested the ability of B-crystallin to suppress the aggregation of a polyQ protein and -synuclein in Drosophila. We found that B-crystallin suppresses both the compound eye degeneration induced by polyQ and the -synuclein-induced rough eye phenotype. Furthermore, by using histochemical staining we have determined that B-crystallin inhibits the aggregation of polyQ in vivo. These data provide a clue for the development of therapeutics for neurodegenerative diseases. Copyright © 2012 Nguyen Trong Tue et al.