Accumulation of amyloid-β in organs results in a series of diseases. Heat shock transcription factor 1 (HSF1) is the master regulator of genes encoding molecular chaperones and attenuates apoptosis induced by multiple factors. However, the role of HSF1 on amyloid-β-induced apoptosis is still unknown. The present study was aimed to explore the function of HSF1 in amyloid-β-induced cardiomyocytes apoptosis. TUNEL assay and flow cytometry analysis were used to detect cell apoptosis. Phalloidin staining was used to detect cytoskeleton injury. Changes in expression levels of proteins involved in apoptosis and endoplasmic reticulum stress were measured by Western blot. In our study, amyloid-β was found to promote apoptosis, impair cytoskeleton, and induce endoplasmic reticulum stress in isolated cardiomyocytes. However, these damaging effects of amyloid-β can be relieved by over-expression of HSF1, and the protective role of HSF1 might be associated with the regulation of HSPs expressions. Results of our study suggest that over-expression of HSF1 might become a promising gene therapeutic for the treatment of heart diseases associated with amyloid-β accumulation.
Keywords: Amyloid-β; Apoptosis; Cardiomyocytes; Heat shock protein; Heat shock transcription factor 1.