Site‐specific mutagenesis of human interleukin‐6 and its biological activity

FEBS Letters

Kishimoto, Tadamitsu¹  Futatsugi, Kensuke²  Nishimura, Chiaki³  Arata, Yoji³  Yasukawa, Kiyoshi² 

[1] Institute for Molecular and Cellular Biology, Osaka University, Suita City, Osaka, Japan;Tasah Corporation, Ayase-shi, Kanagawa, Japan;Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo, Japan

关键词: Interleukin-6;    Site-specific mutagenesis;    B-cell stimulatory activity;    Receptor-binding activity;    Hydrophobic side-chain;    Human;    IL-6;    interleukin-6;    NMR;    nuclear magnetic resonance;    ELISA;    enzyme-linked immunosorbent assay;    Ig;    immunoglobulin;   

DOI  :  10.1016/0014-5793(91)80384-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Amino acid substitutions of human interleukin-6 (IL-6) were performed. Single substitution Met¹⁶² → Ala and double substitutions Leu^{159, 166} → Val resulted in a significant decrease of IL-6 activity in the production of immunoglobulin (lg) from B-cells. Single substitution Leu¹⁶⁶→Val or Leu¹⁵⁹→Val gave a slight or no significant decrease in the Ig-induction activity, respectively. The receptor-binding activity of each IL-6 mutant was also examined. It was observed that the decrease of the receptor-binding activity was generally in parallel with that of the Ig-induction activity. We therefore suggest that hydrophobic side-chains existing in Met¹⁶², Leu¹⁵⁹, and Leu¹⁶⁴ are significantly involved in the receptor-binding of IL-6.

【 授权许可】

Unknown