@article{oai:nagasaki-u.repo.nii.ac.jp:00008397,
 author = {Yahiro, Kinnosuke and Satoh, Mamoru and Nakano, Masayuki and Hisatsune, Junzo and Isomoto, Hajime and Sap, Jan and Suzuki, Hidekazu and Nomura, Fumio and Noda, Masatoshi and Moss, Joel and Hirayama, Toshiya},
 issue = {37},
 journal = {Journal of Biological Chemistry},
 month = {Sep},
 note = {In Helicobacter pylori infection, vacuolating cytotoxin (VacA)-induced mitochondrial damage leading to apoptosis is believed to be a major cause of cell death. It has also been proposed that VacA-induced autophagy serves as a host mechanism to limit toxin-induced cellular damage. Apoptosis and autophagy are two dynamic and opposing processes that must be balanced to regulate cell death and survival. Here we identify the low-density lipoprotein receptor-related protein-1 (LRP1) as the VacA receptor for toxin-induced autophagy in the gastric epithelial cell line AZ-521, and show that VacA internalization through binding to LRP1 regulates the autophagic process including generation of LC3-II from LC3-I, which is involved in formation of autophagosomes and autolysosomes. Knockdown of LRP1 and Atg5 inhibited generation of LC3-II as well as cleavage of PARP, a marker of apoptosis, in response to VacA, whereas caspase inhibitor, benzyloxycarbonyl-VAD- fluoromethylketone (Z-VAD-fmk), and necroptosis inhibitor, Necrostatin-1, did not inhibit VacA-induced autophagy, suggesting that VacA-induced autophagy via LRP1 binding precedes apoptosis. Other VacA receptors such as RPTPα, RPTPβ, and fibronectin did not affect VacA-induced autophagy or apoptosis. Therefore, we propose that the cell surface receptor, LRP1, mediates VacA-induced autophagy and apoptosis., Journal of Biological Chemistry, 287(37), pp.31104-31115; 2012},
 pages = {31104--31115},
 title = {Low-density Lipoprotein Receptor-related Protein-1 (LRP1) Mediates Autophagy and Apoptosis Caused by Helicobacter pylori VacA},
 volume = {287},
 year = {2012}
}