Enhanced Signal Transduction by a Directly Fused Protein of Interleukin-6 and Its Receptor
スポンサーリンク
概要
- 論文の詳細を見る
In order to develop a new type of agonist for the interleukin 6 (IL-6) signal, the gene encoding a directly fused protein (DFP) was constructed by joining the N-terminal portion of IL-6 and the C-terminal (soluble) portion of IL-6R (sIL-6R) without using a flexible polypeptide linker. The biological activity of DFP from a recombinant Pichia pastoris was examined by growth stimulation of IL-6-dependent BAF130 cells expressing human gp130, a membrane receptor. The recombinant DFP exhibited a much stronger growth stimulation (>10 times) than the independent IL-6 and sIL-6R (IL-6/sIL-6R), mainly because association of the IL-6 and IL-6R could be maintained even at lower concentrations of DFP. Surface plasmon resonance (SPR) analysis showed that DFP bound to the extracellular portion of gp130 in the biphasic mode, and the dissociation constants of DFP for two phases were the same as those of IL-6/sIL-6R. In cells treated with DFP, stimulation of Stat3 phosphorylation was maintained for a longer period (>150 min) that in cells treated with IL6/IL-6R, suggesting that the signal mediated by the DFP was more durabler than that mediated by IL-6/sIL-6R, although the signal transduction mechanisms are almost the same for both DFP and IL-6/IL-6R. Therefore, the stronger activity of DFP was attributed to the maintained association of its subunits and/or prolonged phosphorylation of Stat3.
- 社団法人日本生物工学会の論文
- 2001-03-25
著者
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Takagi Masahiro
School Of Materials Science Japan Advanced Institute Of Science And Technology
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FUKUI Kiichi
Department of Biotechnology, Graduate School of Engineering, Osaka University
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Fukui Kiichi
Department Of Biotechnology Graduate School Of Engineering Osaka University
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Takagi M
School Of Materials Science Japan Advanced Institute Of Science And Technology
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Takagi Mutsumi
International Center For Biotechnology Osaka University:(present Address)division Of Biotechnology A
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MIZUNO Haruo
Department of Pediatrics, Neonatology and Congenital Disorders, Nagoya City University Graduate Scho
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IMANAKA Tadayuki
Department of Synthetic and Biological Chemistry, Graduate School of Engineering, Kyoto University
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TAKAGI MASAHIRO
Department of Biotechnology, Graduate School of Engineering, Osaka University
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MIZUGUCHI HIROSHI
Department of Biotechnology, Graduate School of Engineering, Osaka University
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YASUKAWA KIYOSHI
Tokyo Research Center, Tosoh Corporation
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ISHIGURO TAKAHIKO
Tokyo Research Center, Tosoh Corporation
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Mizuno Haruo
Departments Of Pediatrics And Neonatology Nagoya City University Graduate School Of Medical Sciences
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Mizuno Haruo
Department Of Biotechnology Graduate School Of Engineering Osaka University
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Takagi M
Nagasaki Univ. Nagasaki Jpn
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Yasukawa K
Tosoh Corp. Kanagawa Jpn
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Yasukawa Kiyoshi
Tokyo Research Center Tosoh Corporation
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Yasukawa Kiyoshi
Scientific Instruments Division Tosoh Corporation
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Biotechnology Faculty Of Eigineering Osaka University
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Imanaka Tadayuki
Department Of Synthetic And Biological Chemistry Graduate School Of Engineering Kyoto University
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Imanaka T
Department Of Biotechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering.kyoto Univ
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Fukui Kiichi
Department Of Biotechnology Faculty Of Engineering Graduate School Of Osaka University
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Mizuguchi H
Department Of Biochemistry Osaka Medical College
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Ishiguro Takahiko
Tokyo Research Center Tosoh Corporation
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Fujimoto K
Japan Advanced Inst. Of Sci. And Technol. Ishikawa
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Imanaka T
Dep. Of Biotechnology Coll. Of Life Sciences Ritsumeikan Univ.
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Takagi Masahiro
Graduate School Of Biological Sciences Nara Institute Of Science And Technology (naist)
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Takagi Masahiro
Department Of Biotechnology Faculty Of Engineering Osaka University
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Mizuguchi Hiroshi
Department of Biotechnology, Graduate School of Engineering Osaka University
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