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News and Views
Nature Medicine 11, 1052 - 1053 (2005)
doi:10.1038/nm1005-1052
Targeting toxic proteins for turnover
Albert R La Spada1 & Patrick Weydt2
- Albert R. La Spada is in the Departments of Laboratory Medicine, Medicine and Neurology, and The Center for Neurogenetics & Neurotherapeutics, University of Washington, Seattle, Washington 98195, USA. e-mail: laspada@u.washington.edu
- Patrick Weydt is in the Department of Laboratory Medicine, University of Washington, Seattle, Washington 98195, USA.
Abstract
Results now emerge from a preclinical trial of a heat-shock protein inhibitor in a mouse model of neurodegenerative disease. The data indicate that targeting a misfolded protein for degradation may be a useful therapeutic strategy (pages 1088–1095).
Nearly a century ago, Alois Alzheimer observed protein deposits in the brain of a woman with presenile dementia and Friedreich Lewy documented inclusion bodies in the brain of an individual with Parkinson disease. Only relatively recently, however, have neuroscientists realized that such aggregated 'inclusion bodies' are a common feature of almost all neurodegenerative disorders1 and that drugs to eliminate them might be therapeutic.
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