Lu Yi Wei, Ren Yu Dan, Bai Jing, Chen Wei Ning
School of Chemical and Biomedical Engineering, Nanyang Technological University, 62 Nanyang Drive, Singapore 637459.
IUBMB Life. 2008 Oct;60(10):700-2. doi: 10.1002/iub.108.
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.
我们最近报道，乙型肝炎病毒蛋白的天然剪接变体HBSP通过其BH3结构域表现出促凋亡活性。为了研究HBSP中的BH3结构域是否与Bcl-2蛋白家族相互作用，我们在哺乳动物双杂交系统中克隆并表达了HBSP和Bcl-2蛋白家族。在HepG2细胞中进行相互作用测定，并通过报告基因产物荧光素酶的活性进行测量。我们的结果表明，HBSP在体外与Bcl-2/Bcl-xl相互作用，并在HepG2细胞中诱导凋亡。
