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Báo cáo khoa học: "Expression of Angiostatin Using DNA - Based Semliki Forest Virus Replicon"
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Tuyển tập các báo cáo nghiên cứu khoa học quốc tế về bệnh thú y đề tài: Expression of Angiostatin Using DNA - Based Semliki Forest Virus Replicon" | J. Vet. Sci. 2002 3 1 41-45 JOURNAL OF Veterinary Science Expression of Angiostatin Using DNA-Based Semliki Forest Virus Replicon Yong-Soo Choi Jong-Soo Lee Young-Ki Choi Kwang-Soon Shin Hyun-Soo Kim and Chul-Joong Kim College of Veterinary Medicine Chungnam National University Daejon 305-764 Korea ABSTRACT Angiogenesis is recognized as a critical factor in the growth of tumor cells and plays a key role in the tumor metastasis. Recent studies for antiangiogenic substances are getting popular. The angiostatin one of the antiangiogenic substances leads to the increased apoptosis of the tumor cells by inhibiting the neovascularization of the tumor. The angiostatin was identified as the internal fragments of the plasminogen which has no antiangiogenic activity. By hydrolysis of the plasminogen the angiostatin can be produced. In this study we constructed the SFV-derived DNA vector by employing the cytomegalovirus immediate early enhancer promoter CMV . This vector makes it possible to transfect the cells with DNA without the in vitro transcription process. The C-myc epitope and polyhistidine residue sequences were placed in downstream of the angiostatin gene to make it eligible to detect the expressed protein. The murine Ig K -chain V-J2-C signal sequence was placed in upstream to secrete the expressed protein from the cells. We confirmed the expression of angiostatin in the BHK-21 cells using DNA-based SFV replicon. INTRODUCTION Angiogenesis the formation of new vessels from the preexisting microcapillaries is recognized increasingly as a critical factor in a broad spectrum of diseases. The potential therapeutic benefits for the treatment of tumors with antiangiogenic substances therefore are very high 5 . Angiostatin was initially isolated from mice bearing a Lewis lung carcinoma and was identified as a 38 kDa internal fragment of plasminogen that encompasses the first four kringles of the molecule 3 9 7 . The kringles are the conserved domains in a number of plasma