Aspirin-induced Bcl-2 translocation and its phosphorylation in the nucleus trigger apoptosis in breast cancer cells.
- Author:
Bo Hwa CHOI
1
;
Goutam CHAKRABORTY
;
Kwanghee BAEK
;
Ho Sup YOON
Author Information
1. School of Biological Science, Nanyang Technological University, Singapore, Singapore. hsyoon@ntu.edu.sg
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
apoptosis;
aspirin;
Bcl-2;
breast cancer;
FKBP38;
MCF-7
- MeSH:
Active Transport, Cell Nucleus/drug effects;
*Apoptosis;
Aspirin/*pharmacology;
Cell Nucleus/*metabolism;
Humans;
MCF-7 Cells;
Phosphorylation;
Protein Binding;
Proto-Oncogene Proteins c-bcl-2/genetics/*metabolism;
Tacrolimus Binding Proteins/metabolism
- From:Experimental & Molecular Medicine
2013;45(10):e47-
- CountryRepublic of Korea
- Language:English
-
Abstract:
Here, we report that B-cell lymphoma 2 (Bcl-2) is a novel target molecule of aspirin in breast cancer cells. Aspirin influenced the formation of a complex by Bcl-2 and FKBP38 and induced the nuclear translocation of Bcl-2 and its phosphorylation. These events inhibited cancer cell proliferation and subsequently enhanced MCF-7 breast cancer cell apoptosis. Bcl-2 knockdown using small interfering RNA (siRNA) delayed apoptotic cell death, which correlated with increased proliferation following aspirin exposure. In contrast, Bcl-2 overexpression enhanced the onset of aspirin-induced apoptosis, which was also associated with a significant increase in Bcl-2 phosphorylation in the nucleus. Therefore, this study may provide novel insight into the molecular mechanism of aspirin, particularly its anticancer effects in Bcl-2- and estrogen receptor-positive breast cancer cells.
