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beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor.

We characterized beta-synuclein, the non-amyloidogenic homolog of alpha-synuclein, as an inhibitor of aggregation of alpha-synuclein, a molecule implicated in Parkinson's disease. For this, doubly transgenic mice expressing human (h) alpha- and beta-synuclein were generated. In doubly transgenic mice, beta-synuclein ameliorated motor deficits, neurodegenerative alterations, and neuronal alpha-synuclein accumulation seen in halpha-synuclein transgenic mice. Similarly, cell lines transfected with beta-synuclein were resistant to alpha-synuclein accumulation. halpha-synuclein was coimmunoprecipitated with hbeta-synuclein in the brains of doubly transgenic mice and in the double-transfected cell lines. Our results raise the possibility that beta-synuclein might be a natural negative regulator of alpha-synuclein aggregation and that a similar class of endogenous factors might regulate the aggregation state of other molecules involved in neurodegeneration. Such an anti-amyloidogenic property of beta-synuclein might also provide a novel strategy for the treatment of neurodegenerative disorders.

Pubmed ID: 11683992


  • Hashimoto M
  • Rockenstein E
  • Mante M
  • Mallory M
  • Masliah E



Publication Data

October 25, 2001

Associated Grants

  • Agency: NIA NIH HHS, Id: AG10689
  • Agency: NIA NIH HHS, Id: AG18440
  • Agency: NIA NIH HHS, Id: AG5131

Mesh Terms

  • Animals
  • Antiparkinson Agents
  • Brain
  • Dimerization
  • Gene Expression
  • Humans
  • Immunosorbent Techniques
  • Mice
  • Mice, Inbred C57BL
  • Mice, Inbred DBA
  • Mice, Transgenic
  • Motor Activity
  • Nerve Tissue Proteins
  • Neurodegenerative Diseases
  • Recombinant Proteins
  • Synucleins
  • Transfection
  • alpha-Synuclein
  • beta-Synuclein