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Originally published In Press as doi:10.1074/jbc.M700053200 on May 24, 2007

J. Biol. Chem., Vol. 282, Issue 30, 21618-21628, July 27, 2007
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Bax Inhibitor-1 Regulates Endoplasmic Reticulum Stress-associated Reactive Oxygen Species and Heme Oxygenase-1 Expression*Formula

Geum-Hwa Lee{ddagger}, Hyun-Kyung Kim§, Soo-Wan Chae{ddagger}, Do-Sung Kim{ddagger}, Ki-Chan Ha{ddagger}, Mike Cuddy||, Christina Kress||, John C. Reed||, Hyung-Ryong Kim§1, and Han-Jung Chae{ddagger}2

From the {ddagger}Department of Pharmacology and Institute of Cardiovascular Research, School of Medicine, Chonbuk National University, Jeonju, Chonbuk 561-182, South Korea, the §Department of Dental Pharmacology and Wonkwang Biomaterial Implant Research Institute, School of Dentistry, Wonkwang University, Iksan, Chonbuk 570-749, South Korea, the Clinical Trial Center for Functional Foods, Chonbuk Hospital, Jeonju, Chonbuk South Korea, and the ||Burnham Institute for Medical Research, La Jolla, California 02037

The Bax inhibitor-1 (BI-1) is an anti-apoptotic protein that is located in endoplasmic reticulum (ER) membranes and protects cells from ER stress-induced apoptosis. The ER is associated with generation of reactive oxygen species (ROS) through oxidative protein folding. This study examined the role of BI-1 in the regulation of ER stress-induced accumulation of ROS and expression of unfolded protein response-associated proteins. BI-1 reduced the expression levels of glucose response protein 78, C/EBP homologous protein, phospho-eukaryotic initiation factor 2{alpha}, IRE1{alpha}, XBP-1, and phospho-JNK and inhibited the cleavage of ATF-6{alpha} p-90, leading to the inhibition of ROS. Although ROS scavengers offer some protection against ER stress-induced apoptosis, the expression of pro-apoptotic ER stress proteins was not affected. This study shows that the response of unfolded proteins is followed by ROS accumulation under ER stress, which is regulated in BI-1 cells. The mechanism for these BI-1-associated functions involves the expression of heme oxygenase-1 (HO-1) through nuclear factor erythroid 2-related factor 2. In BI-1 cells, the transfection of HO-1 small interfering RNA completely abolished the BI-1-induced protection. The endogenous expression of HO-1 through ER stress-initiated ROS is believed to be as a protection signal. In conclusion, these observations suggest that BI-1 can inhibit the ER stress proteins as well as the accumulation of ROS, thereby protecting the cells. Moreover, HO-1 plays an important role in the BI-1-associated protection against ER stress.


Received for publication, January 3, 2007 , and in revised form, May 24, 2007.

* This work was supported by Korea Science and Engineering Foundation Grant R01-2006-000-10422-0 and Korean Research Foundation Grant KRF-2005-E00021 funded by the Korean Government. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S3 and supplemental Tables S1 and S2.

1 To whom correspondence may be addressed: Dept. of Dental Pharmacology, School of Dentistry, Wonkwang University, Iksan, Chonbuk, South Korea. Tel.: 82-63-850-6640; Fax: 82-63-854-0285; E-mail: hrkimdp{at}wonkwang.ac.kr.

2 To whom correspondence may be addressed: Dept. of Pharmacology & Institute of Cardiovascular Research, Medical School, Chonbuk University, Jeonju, Chonbuk, South Korea. Tel.: 82-63-270-3092; Fax: 82-63-275-2855; E-mail: hjchae{at}chonbuk.ac.kr.


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