Site-specific mutagenesis of human interleukin-6 and its biological activity |
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| Authors: | C Nishimura K Futatsugi K Yasukawa T Kishimoto Y Arata |
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| Affiliation: | Faculty of Pharmaceutical Sciences, University of Tokyo, Japan. |
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| Abstract: | Amino acid substitutions of human interleukin-6 (IL-6) were performed. Single substitution Met162----Ala and double substitutions Leu159.166----Val resulted in a significant decrease of IL-6 activity in the production of immunoglobulin (Ig) 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 Leu166 are significantly involved in the receptor-binding of IL-6. |
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