Effect of αB-crystallin on protein aggregation in Drosophila

J Biomed Biotechnol. 2012;2012:252049. doi: 10.1155/2012/252049. Epub 2012 Mar 7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry*
  • Amyloid / metabolism*
  • Animals
  • Animals, Genetically Modified / genetics
  • Animals, Genetically Modified / metabolism
  • Drosophila
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Eye / chemistry
  • Eye / cytology
  • Immunohistochemistry
  • Microscopy, Electron, Scanning
  • Peptides / chemistry
  • Peptides / metabolism
  • Protein Binding
  • alpha-Crystallin B Chain / chemistry*
  • alpha-Crystallin B Chain / genetics
  • alpha-Crystallin B Chain / metabolism*
  • alpha-Synuclein / chemistry
  • alpha-Synuclein / genetics
  • alpha-Synuclein / metabolism


  • Amyloid
  • Drosophila Proteins
  • Peptides
  • alpha-Crystallin B Chain
  • alpha-Synuclein
  • polyglutamine