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FEBS Lett. 2002 Mar 27;515(1-3):61-5.

Mutant huntingtin aggregates do not sensitize cells to apoptotic stressors.

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1
Department of Psychiatry and Behavioral Neurobiology, 1720 7th Avenue South, SC1061, University of Alabama at Birmingham, School of Medicine, Birmingham, AL 35294-0017, USA.

Abstract

It has been postulated that neuronal inclusions composed of mutant huntingtin may play a causative role in the pathogenesis of Huntington's disease. To study the putative role of aggregates in modulating apoptotic vulnerability, SH-SY5Y cell lines stably expressing truncated huntingtin with 18 (wild-type) (N63-18Q) or 82 (mutant) (N63-82Q) glutamine repeats were established. Aggregates were observed in approximately 13% of the N63-82Q cells; no aggregates were observed in the N63-18Q cells. In response to apoptotic stimuli such as staurosporine or hyperosmotic stress, caspase-3 activity was significantly greater in the N63-82Q cells compared to the N63-18Q cells. However, double immunostaining for huntingtin and active caspase-3 revealed that the presence of aggregates did not correlate with the presence of active caspase-3, indicating that aggregates do not contribute to the increase in apoptosis in the N63-82Q cells.

PMID:
11943195
DOI:
10.1016/s0014-5793(02)02436-5
[Indexed for MEDLINE]
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