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Trehalose alleviates polyglutamine-mediated pathology in mouse model of Huntington disease

Nat Med. 2004 Feb;10(2):123-4.

Tanaka M, Machida Y, Niu S, Ikeda T, Jana NR, Doi H, Kurosawa M, Nekooki M,
Nukina N. Laboratory for Structural Neuropathology, RIKEN Brain Science
Institute, 2-1 Hirosawa, Wako City, Saitama 351-0198, Japan.

Abstract:

Inhibition of polyglutamine-induced protein aggregation could provide treatment
options for polyglutamine diseases such as Huntington disease. Here we showed
through in vitro screening studies that various disaccharides can inhibit
polyglutamine-mediated protein aggregation. We also found that various
disaccharides reduced polyglutamine aggregates and increased survival in a cellular
model of Huntington disease. Oral administration of trehalose, the most effective of
these disaccharides, decreased polyglutamine aggregates in cerebrum and liver,
improved motor dysfunction and extended lifespan in a transgenic mouse model of
Huntington disease. We suggest that these beneficial effects are the result of
trehalose binding to expanded polyglutamines and stabilizing the partially unfolded
polyglutamine-containing protein. Lack of toxicity and high solubility, coupled with
efficacy upon oral administration, make trehalose promising as a therapeutic drug
or lead compound for the treatment of polyglutamine diseases. The saccharidepolyglutamine
interaction identified here thus provides a new therapeutic strategy for
polyglutamine diseases.

Last Updated ( May 02, 2008 at 11:28 AM )