Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract.

摘要: Spinal and bulbar muscular atrophy (SBMA) is one of a group human inherited neurodegenerative diseases caused by polyglutamine expansion. We have previously demonstrated that the SBMA gene product, androgen receptor protein, toxic aggregates when truncated. Heat shock proteins function as molecular chaperones, which recognize renaturate misfolded protein (aggregate). thus assessed effect variety chaperones in cultured neuronal cell model SBMA. Overexpression reduces aggregate formation suppresses apoptosis to differing degrees depending on their combinations. Combination Hsp70 Hsp40 was most effective among reducing providing cellular protection, reflecting act together chaperoning mutant disabled proteins. Although Hdj2/Hsdj chaperone has been reported suppress expanded tract-formed aggregate, Hsdj/Hdj2 showed little our system. These findings indicate may be key factors developing CAG repeat disease suggested increasing expression level or enhancing will provide an avenue for treatment disease.