Bowman AB, Yoo SY, Dantuma NP, Zoghbi HY. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitin-proteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum Mol Genet. 2005 Mar 1;14(5):679-91. PubMed.

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  1. This paper reports additional evidence that nuclear inclusions of polyglutamine-containing proteins may actually be protective because they may segregate and inactivate the free mutant proteins (for example, huntingtin), which may be more toxic to the cell than are their aggregates. Thus, protein aggregation may not necessarily be a toxic process and may actually play a cell-protective role in Huntington disease and spinocerebellar ataxias. The similarities to the Alzheimer disease (AD) field are clear because this field is finally accepting the notion that the amyloid-β aggregates are not the main neurotoxic agent that drives the AD neurodegeneration (see Neve and Robakis, 1998).

    References:

    Neve RL, Robakis NK. Alzheimer's disease: a re-examination of the amyloid hypothesis. Trends Neurosci. 1998 Jan;21(1):15-9. PubMed.

    View all comments by Nikolaos K. Robakis

  2. Please access article in Nature news July 2004 re "Lithium may fend off Alzheimer's disease". It is available to Premium Plus subscribers to news@nature.com, available to institutions or at a rate of 15.99 per month.

    Both my deceased brother and myself were prescribed lithium. My father at age 84 is showing Alzheimer's symptoms. Those of us still alive would gladly give research scientists access to our blood and in my own case (under the direction of my doctors) other scientific tests if this could lead to a cure for Alzheimer disease.

    View all comments by Susan R Saslaw

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  1. Polyglutamine, Inclusion Bodies and the Proteasome—The Good, the Bad, and the Innocent?