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Carcinogenesis Advance Access originally published online on February 6, 2008
Carcinogenesis 2008 29(4):729-737; doi:10.1093/carcin/bgn036
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© The Author 2008. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Interactions of acetylcholinesterase with caveolin-1 and subsequently with cytochrome c are required for apoptosome formation

Sang Eun Park1,3, Seung Hun Jeong1, Soo-Bog Yee1, Tae Hyun Kim1, Young Hwa Soung1, Nam Chul Ha2, Nam Deuk Kim3, Jae-Yong Park4, Hae Rahn Bae5, Bong Soo Park6, Hye Jeong Lee7 and Young Hyun Yoo1,*

1 Department of Anatomy and Cell Biology, Dong-A University College of Medicine and Medical Science Research Center, Busan 602-714, South Korea
2 Department of Manufacturing Pharmacy (BK21 Program)
3 Department of Pharmacy (BK21 Program), The Graduate School, Pusan National University, Busan 609-735, South Korea
4 Department of Physiology, Institute of Health Science and Medical Research Center for Neural Dysfunction, Gyeongsang National University School of Medicine, Jinju 660-751, South Korea
5 Department of Physiology, Dong-A University College of Medicine and Medical Science Research Center, Busan 602-714, South Korea
6 Department of Oral Anatomy and Cell Biology, College of Dentistry, Pusan National University, Busan 602-735, South Korea
7 Department of Pharmacology, Dong-A University College of Medicine and Medical Science Research Center, Busan 602-714, South Korea

* To whom correspondence should be addressed. Tel: +82 51 240 2926; Fax: +82 51 241 3767; Email: yhyoo{at}dau.ac.kr

Acetylcholinesterase (AChE) is emerging as an important component in leading to apoptosis. Our previous study demonstrated that silencing of the AChE gene blocked the interaction between cytochrome c and apoptotic protease-activating factor-1 (Apaf-1) in etoposide-induced apoptosis of HT-29 cells. We undertook this study to further dissect the molecular role of AChE in apoptosome formation. The present study elicited that small interfering RNA (siRNA) to cytochrome c gene blocked the interaction of AChE with Apaf-1, whereas siRNA to Apaf-1 gene did not block the interaction of AChE with cytochrome c, indicating that the interaction of AChE with cytochrome c is required for the interaction between cytochrome c and protease-activating factor-1. We further observed that AChE is localized to caveolae via interacting with caveolin-1 during apoptosis and that the disruption of caveolae prevented apoptosome formation. These data indicate that the interactions of AChE with caveolin-1 and subsequently with cytochrome c appear to be indispensable for apoptosome formation.

Abbreviations: AChE, acetylcholinesterase; Apaf-1, apoptotic protease-activating factor-1; EGFP, enhanced green fluorescent protein; LMB, leptomycin B; MβCD, methyl-β-cyclodextrin; siRNA, small interfering RNA

Received November 30, 2007; revised January 17, 2008; accepted January 26, 2008.


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