Role of leucine residues in the C‐terminal region of human interleukin‐6 in the biological activity

FEBS Letters

Ekida, Teiji²  Nomura, Kazuhide²  Sakamoto, Koji²  Kishimoto, Tadamitsu¹  Nishimura, Chiaki²  Arata, Yoji²  Suzuki, Hiroshi³  Yasukawa, Kiyoshi³ 

[1] Department of Medicine III, Osaka University Medical School, Fukushima-ku, Osaka, Japan;Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo, Japan;Tosoh Corporation, Ayase-shi, Kanagawa, Japan

关键词: Interleukin 6;    Site-directed mutagenesis;    Peptide fragment;    Receptor-binding activity;    B-Cell stimulatory activity;    Human;    IL-6;    interleukin-6;    E. coli;    Escherichia coli;    Ig;    immunoglobulin;    hGH;    human growth hormone;    ELISA;    enzyme-linked immunosorbent assay;   

DOI  :  10.1016/0014-5793(92)81118-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Site-directed mutagenesis of two sets of three periodic leucine residues which appear at every seventh position in the C-terminal region of human interleukin-6 (IL-6) was performed. Both receptor-binding and immunoglobulin (Ig)-induction activities of a triple mutant Leu^168,175,182→Val were only 1% compared with those of wild-type IL-6. However, the mutant Leu^152,159,166→Val had 13% receptor-binding and 2% Ig-induction activities of those of wild-type IL-6. In order to obtain more direct information on the receptor-binding region, we prepared two synthetic peptides. A significant binding activity was observed for the peptide Leu¹⁶⁸-Met¹⁸⁵, but not for the peptide Leu¹⁵²-Arg¹⁶⁹. These results indicate that leucine residues in the C-terminal region, especially Leu¹⁶⁸, Leu¹⁷⁵, and Leu¹⁸², play an important role in the receptor-binding and Ig-induction activities.

【 授权许可】

Unknown