Effect ofαB-Crystallin on Protein Aggregation inDrosophila

[摘要] Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression ofα-synuclein, underlie neurodegenerative diseases including Alzheimer’s, Parkinson, Huntington, Creutzfeldt diseases. Small heat-shock proteins, such asαB-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 ofαB-crystallin to suppress the formation of protein aggregates. We tested the ability ofαB-crystallin to suppress the aggregation of a polyQ protein andα-synuclein inDrosophila. We found thatαB-crystallin suppresses both the compound eye degeneration induced by polyQ and theα-synuclein-induced rough eye phenotype. Furthermore, by using histochemical staining we have determined thatαB-crystallin inhibits the aggregation of polyQin vivo. These data provide a clue for the development of therapeutics for neurodegenerative diseases.

[学科分类] 基础医学