Journal Article

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

Sang Eun Park, Seung Hun Jeong, Soo-Bog Yee, Tae Hyun Kim, Young Hwa Soung, Nam Chul Ha, Nam Deuk Kim, Jae-Yong Park, Hae Rahn Bae, Bong Soo Park, Hye Jeong Lee and Young Hyun Yoo

in Carcinogenesis

Volume 29, issue 4, pages 729-737
Published in print April 2008 | ISSN: 0143-3334
Published online February 2008 | e-ISSN: 1460-2180 | DOI: http://dx.doi.org/10.1093/carcin/bgn036
Interactions of acetylcholinesterase with caveolin-1 and subsequently with cytochrome c are required for apoptosome formation

More Like This

Show all results sharing this subject:

  • Clinical Cytogenetics and Molecular Genetics

GO

Show Summary Details

Preview

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.

Journal Article.  5575 words.  Illustrated.

Subjects: Clinical Cytogenetics and Molecular Genetics

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.