@article{oai:kanazawa-u.repo.nii.ac.jp:00013486,
 author = {Hori, Osamu and Ichinoda, Fusae and Tamatani, Takashi and Yamaguchi, Atsushi and Sato, Naoya and Ozawa, Kentaro and Kitao, Yasuko and Miyazaki, Mayuki and Harding, Heather P. and Ron, David and Tohyama, Masaya and Stern, David M. and Ogawa, Satoshi},
 issue = {7},
 journal = {Journal of Cell Biology},
 month = {Jun},
 note = {The rat homologue of a mitochondrial ATP-dependent protease Lon was cloned from cultured astrocytes exposed to hypoxia. Expression of Lon was enhanced in vitro by hypoxia or ER stress, and in vivo by brain ischemia. These observations suggested that changes in nuclear gene expression (Lon) triggered by ER stress had the potential to impact important mitochondrial processes such as assembly and/or degradation of cytochrome c oxidase (COX). In fact, steady-state levels of nuclear-encoded COX IV and V were reduced, and mitochondrial-encoded subunit II was rapidly degraded under ER stress. Treatment of cells with cycloheximide caused a similar imbalance in the accumulation of COX subunits, and enhanced mRNA for Lon and Yme1, the latter another mitochondrial ATP-dependent protease. Furthermore, induction of Lon or GRP75/mtHSP70 by ER stress was inhibited in PERK (-/-) cells. Transfection studies revealed that overexpression of wild-type or proteolytically inactive Lon promoted assembly of COX II into a COX I-containing complex, and partially prevented mitochondrial dysfunction caused by brefeldin A or hypoxia. These observations demonstrated that suppression of protein synthesis due to ER stress has a complex effect on the synthesis of mitochondrial-associated proteins, both COX subunits and ATP-dependent proteases and/or chaperones contributing to assembly of the COX complex.},
 pages = {1151--1160},
 title = {Transmission of cell stress from endoplasmic reticulum to mitochondria: Enhanced expression of Lon protease},
 volume = {157},
 year = {2002}
}