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Heat shock protein 70 (Hsp70) is an ATP\u2010dependent molecular chaperone and exhibits an anti\u2010apoptosis ability in a variety of cells. Previous studies reported that the expression of Hsp70 was induced when organisms were exposed to FA. Whether Hsp70 plays a role in the FA\u2010induced apoptosis and the involved cell signaling pathway remain largely unknown. In this study, human bronchial epithelial cells with overexpressed Hsp70 and the control were exposed to different concentrations of FA (0, 40, 80, and 160\u2009\u03bcmol\/L) for 24\u2009hours. Apoptosis and the expression levels of PI3K, Akt, p\u2010Akt, MEK, p\u2010MEK, and GLI2 were detected by Annexin\u2010APC\/7AAD double\u2010labeled flow cytometry and western blot. The results showed that overexpression of Hsp70 decreased the apoptosis induced by FA and alleviated the decline of PI3k and p\u2010Akt significantly. Inhibitor (LY 294002, a specific inhibitor of PI3K\u2010Akt) test result indicated that PI3K\u2010Akt signaling pathway was involved in the inhibition of FA\u2010induced apoptosis by Hsp70 overexpression and also active in the maintenance of GLI2 level. However, it also suggested that other signaling pathways activated by overexpressed Hsp70 participated in this process, which was needed to be elucidated in further research.<\/jats:p>","DOI":"10.1002\/tox.22703","type":"journal-article","created":{"date-parts":[[2019,1,2]],"date-time":"2019-01-02T08:43:34Z","timestamp":1546418614000},"page":"495-504","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Overexpressed Hsp70 alleviated formaldehyde\u2010induced apoptosis partly via PI3K\/Akt signaling pathway in human bronchial epithelial cells"],"prefix":"10.1002","volume":"34","author":[{"given":"Lulu","family":"Liu","sequence":"first","affiliation":[{"name":"Department of Occupational and Environmental Health, Xiangya School of Public Health Central South University  Changsha 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