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Hsp70 acetylation prevents caspase-dependent/independent apoptosis and autophagic cell death in cancer cells

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Affiliated Author(s)
서지혜
Alternative Author(s)
Seo, Ji Hye
Journal Title
International Journal of Oncology
ISSN
1019-6439
Issued Date
2017
Abstract
Cancer cells are continuously challenged by adverse environmental factors including hypoxia, metabolite restriction, and immune reactions, and must adopt diverse strategies to survive. Heat shock protein (Hsp) 70 plays a central role in protection against stress-induced cell death by maintaining protein homeostasis and interfering with the process of programmed cell death. Recent findings have suggested that Hsp70 acetylation is a key regulatory modification required for its chaperone activity, but its relevance in the process of programmed cell death and the underlying mechanisms involved are not well understood. In this study, we sought to investigate mechanisms mediated by Hsp70 acetylation in relation to apoptotic and autophagic programmed cell death. Upon stress-induced apoptosis, Hsp70 acetylation inhibits apoptotic cell death, mediated by Hsp70 association with apoptotic protease-activating factor (Apaf)-1 and apoptosis-inducing factor (AIF), key modulators of caspase-dependent and -independent apoptotic pathways, respectively. Hsp70 acetylation also attenuated autophagic cell death associated with upregulation of autophagy-related genes and autophagosome induction. Collectively, these results suggest that the acetylation of Hsp70 plays key regulatory roles in cell death pathways as well as in its function as a chaperone, together enabling cellular protection in response to stress.
Department
Dept. of Biochemistry (생화학)
Publisher
School of Medicine (의과대학)
Citation
International Journal of Oncology, Vol.51(2) : 573-578, 2017
Type
Article
DOI
10.3892/ijo.2017.4039
URI
http://kumel.medlib.dsmc.or.kr/handle/2015.oak/41280
Appears in Collections:
1. School of Medicine (의과대학) > Dept. of Biochemistry (생화학)
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