Abstract:
:Striatal neuronal cell death is one of the pathological features of Huntington's disease (HD). Overexpression of some heat shock proteins (HSPs) has been reported to suppress the aggregate formation of mutant huntingtin and concurrent cell death. Heat shock transcription factor-1 (HSF 1), a major transcription factor of HSPs, has also been reported to be increased in HD models. However, the exact role of HSF 1 in the pathogenesis of HD has not been clearly elucidated. 3-Nitropropionic acid (3NP), an irreversible inhibitor of the mitochondrial complex II, induces selective damage to the striatum in animals and produces clinical features of HD. To investigate roles of HSF 1 on 3NP-induced oxidative stress, HSF 1 was transiently overexpressed in striatal cells. Expression of HSF 1 significantly attenuated 3NP-induced apoptotic striatal cell death and resulted in increased expression of HSP 70. Furthermore, expression of HSF 1 significantly attenuated 3NP-induced intracellular reactive oxygen species (ROS) generation. Taken together, the present study clearly demonstrates that HSF 1 attenuates 3NP-induced apoptotic striatal cell death and ROS generation, possibly through HSP70 expression, suggesting that HSF 1 might be a valuable therapeutic target in the treatment of HD.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Choi YJ,Om JY,Kim NH,Chang JE,Park JH,Kim JY,Lee HJ,Kim SS,Chun Wdoi
10.1007/s11010-012-1528-zsubject
Has Abstractpub_date
2013-03-01 00:00:00pages
59-67issue
1-2eissn
0300-8177issn
1573-4919journal_volume
375pub_type
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