Durk Pearson & Sandy Shaw’s®
Life Extension NewsTM
Volume 16 No. 1 • January 2013


Trehalose inhibits aggregation of mutant alpha-synuclein (thought to be a key factor in the cause of Parkinson’s disease) and disaggregates existing fibrils

We have written about the healthful effects of the natural osmolyte trehalose before, once in our writeup on osmolyte protection against protein misfolding (see “The Origami of Aging” in the September 2008 issue of Life Enhancement) and also in our Sept. 2012 (Vol. 15 No. 5) issue of this newsletter. Here we describe a new paper on trehalose1 in which it is reported that trehalose inhibits the aggregation of mutant alpha-synuclein that is believed to be a cause of Parkinson’s disease due to its neurotoxic effects for dopaminergic neurons. Moreover, trehalose was also shown in this study to disaggregate existing aggregated alpha-synuclein fibrils. The authors1 suggest that trehalose “might hold the promise as a novel treatment for PD [Parkinson’s disease], a strategy which has been similarly investigated in other neurodegenerative disorders.” As this work was done in vitro, the authors note that in vivo follow-up work will be required to evaluate its potential in treating PD.

The authors explore other papers that have been published on trehalose, including one that showed trehalose to have autophagy-enhancing effects (helping to clear away unwanted and/or neurotoxic debris), antiinflammatory effects, to slow aging in C. elegans, and to reduce the formation of polyglutamine aggregates and motor dysfunction in a transgenic mouse model of Huntington’s disease (another disorder involving abnormal protein deposits in the brain). The authors report that studies of trehalose for treating PD in vivo (presumably in animal models) are under way.

Reference

  1. Yu et al. Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils. Arch Biochem Biophys 523:144-150 (2012).

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