Researchers from Eliezer Masliah's lab at University of California, San Diego, report that β-synuclein can prevent, and even reverse, the aggregation of the α-isoform. Their evidence comes from in vivo, cell culture, and biochemical experiments. Transgenic mice expressing human α-synuclein exhibited signs of neurodegeneration; a loss of dopaminergic nerve terminals, the presence of inclusion bodies, and loss of locomotor activity. Double transgenics expressing both α- and β-synuclein, however, had close to normal locomotor activity, four-fold fewer inclusion bodies, and wildtype levels of dopaminergic terminals. In addition, α- and β-isoforms co-immunoprecipitated from bitransgenic tissues and from cultured cells coexpressing both isoforms, while in vitro the addition of β-synuclein to α-synuclein aggregates converted most of the α form to monomers.

"This paper is very helpful to the field," says Michael Schlossmacher, at Brigham and Women's Hospital, Boston. "It reports a strong behavioral and morphological modulation, and the coexpression of β-synuclein certainly seems to ameliorate the phenotype."-Tom Fagan.

Reference:Hashimoto M, Rockenstein E, Mante M, Mallory M, Masliah E. b-synuclein inhibits a-synuclein aggregation: A possible role as an anti-Parkinsonian factor. Neuron 2001 October 25;(32):213-223. Abstract

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