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Lysosome Dysfunction Enhances Oxidative Stress‐Induced Apoptosis through Ubiquitinated Protein Accumulation in Hela Cells
Author(s) -
Yu Chunyan,
Huang Xiaowei,
Xu Ye,
LI Hongyan,
Su Jing,
Zhong Jiateng,
Kang Jinsong,
Liu Yuhe,
Sun Liankun
Publication year - 2013
Publication title -
the anatomical record: advances in integrative anatomy and evolutionary biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.678
H-Index - 62
eISSN - 1932-8494
pISSN - 1932-8486
DOI - 10.1002/ar.22612
Subject(s) - menadione , autophagy , hela , oxidative stress , microbiology and biotechnology , endoplasmic reticulum , lysosome , apoptosis , reactive oxygen species , unfolded protein response , mitochondrion , chemistry , oxidative phosphorylation , biology , biochemistry , cell , enzyme
The role of lysosomal system in oxidative stress‐induced apoptosis in cancer cells is not fully understood. Menadione is frequently used as oxidative stress model. It is indicated that menadione could induce autophagy in Hela cells. In the present study, we examined whether the lysosomal inhibitor, ammonium chloride (NH 4 Cl) could prevent the autophagy flux by inhibiting the fusion of autophagosomes with lysosomes and enhance apoptosis induced by menadione via mitochondrial pathway. The results demonstrated generation and accumulation of reactive oxygen species and increased levels of ubiquitinated proteins and GRP78 in cells treated with both menadione and NH 4 Cl. Our data indicates that lysosomal system through autophagy plays an important role in preventing menadione‐induced apoptosis in Hela cells by clearing misfolded proteins, which alleviates endoplasmic reticulum stress. Anat Rec, 2013. © 2012 Wiley Periodicals, Inc.