Effect of αB-Crystallin on Protein Aggregation in Drosophila

Abstract EN

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.