期刊
NEUROSCIENCE LETTERS
卷 378, 期 3, 页码 171-175出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2004.12.031
关键词
polyglutamine; BAG-1; huntingtin; Hsc70/Hsp70
Huntington's disease (HD) is characterised by the proteolytic production of N-terminal fragments of huntingtin containing polyglutamine repeats that forms intracellular ubiquitinated aggregates in the affected neurons. Using cellular and transgenic mice model of HD, we report here that BAG-1 co-immunoprecipitates with the polyglutamine-expanded truncated N-terminal huntingtin (tNhtt) and associates with their aggregates through its interaction with the chaperones Hsc70/Hsp70. We further demonstrate that the over expression of BAG-1 protects polyglutamine-expanded tNhtt induced cell death. Since, BAG-1 is essential for cell survival, its association with tNhtt aggregates might disrupt its normal function and thereby promote polyglutamine-expanded tNhtt-induced cell death. (c) 2004 Elsevier Ireland Ltd. All rights reserved.
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