title: Effect of αB-crystallin on protein aggregation in Drosophila.
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.
authors.affiliation: Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan.
authors.forename: Nguyen Trong
authors.initials: NT
authors.lastname: Tue
authors.forename: Kouhei
authors.initials: K
authors.lastname: Shimaji
authors.forename: Naoki
authors.initials: N
authors.lastname: Tanaka
authors.forename: Masamitsu
authors.initials: M
authors.lastname: Yamaguchi
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D030801:Animals, Genetically Modified / Q000235:genetics / Q000378:metabolism; D004330:Drosophila; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005123:Eye / Q000737:chemistry / Q000166:cytology; D007150:Immunohistochemistry; D008855:Microscopy, Electron, Scanning; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D038203:alpha-Crystallin B Chain / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051844:alpha-Synuclein / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D000682:Amyloid; D029721:Drosophila Proteins; D010455:Peptides; D038203:alpha-Crystallin B Chain; D051844:alpha-Synuclein; C097188:polyglutamine