Abstract
We have recently reported that the naturally occurring spliced variant of Hepatitis B virus protein, HBSP, displayed proapoptotic activity through its BH3 domain. To investigate whether the BH3 domain in HBSP interacted with Bcl-2 family of proteins, HBSP and Bcl-2 family of proteins were cloned and expressed in our mammalian two-hybrid system. Interaction assays were carried out in HepG2 cells and measured by the activity of the reporter gene product luciferase. Our results indicated that HBSP interacted with Bcl-2/Bcl-xl in vitro and induced apoptosis in HepG2 cells.
Original language | English |
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Pages (from-to) | 700-702 |
Number of pages | 3 |
Journal | IUBMB Life |
Volume | 60 |
Issue number | 10 |
DOIs | |
Publication status | Published - 2008 |
Externally published | Yes |
ASJC Scopus Subject Areas
- Biochemistry
- Molecular Biology
- Genetics
- Clinical Biochemistry
- Cell Biology
Keywords
- Apoptosis
- Protein function