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Citation
Tue, N.T., Shimaji, K., Tanaka, N., Yamaguchi, M. (2012). Effect of αB-Crystallin on Protein Aggregation in Drosophila.  J. Biomed. Biotechnol. 2012(): 252049.
FlyBase ID
FBrf0218055
Publication Type
Research paper
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.

PubMed ID
PubMed Central ID
PMC3312385 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Biomed. Biotechnol.
    Title
    Journal of Biomedicine & Biotechnology
    Publication Year
    2001-
    ISBN/ISSN
    1110-7243
    Data From Reference
    Alleles (4)
    Genes (4)
    Human Disease Models (3)
    Natural transposons (1)
    Experimental Tools (2)
    Transgenic Constructs (4)