ArticleMolecular and cellular biochemistry2013
Heat shock transcription factor-1 suppresses apoptotic cell death and ROS generation in 3-nitropropionic acid-stimulated striatal cells.
Article in Molecular and cellular biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Oxidative Stress in Huntington's Disease.Biomolecules · 2025Review
- Heat shock factor 1 drives regulatory T-cell induction to limit murine intestinal inflammation.Mucosal immunology · 2024Article
- Biomimetic Copper-Doped Polypyrrole Nanoparticles for Enhanced Cancer Low-Temperature Photothermal Therapy.International journal of nanomedicine · 2023Article
- The NOR1/OSCP1 proteins in cancer: from epigenetic silencing to functional characterization of a novel tumor suppressor.Journal of Cancer · 2017Review
- Dihydromyricetin Ameliorates 3NP-induced Behavioral Deficits and Striatal Injury in Rats.Journal of molecular neuroscience : MN · 2016Article
- Article
- Mitochondrial succinate dehydrogenase is involved in stimulus-secretion coupling and endogenous ROS formation in murine beta cells.Diabetologia · 2015Article
- Geldanamycin attenuates 3‑nitropropionic acid‑induced apoptosis and JNK activation through the expression of HSP 70 in striatal cells.International journal of molecular medicine · 2014Article
- Eye-specific gene expression following embryonic ethanol exposure in zebrafish: roles for heat shock factor 1.Reproductive toxicology (Elmsford, N.Y.) · 2014Article
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9 authors.
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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.
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