Isolation and bioactivities of three IL-1β N-terminal variants

Abstract

Three distinct N-terminal variants of rhIL-1β can be generated by expression of the IL-1β gene in E. coli; the naturally occurring Ala1 species, Met0-Ala1 and des-Ala1 proteins. Since most studies with rhIL-1β have used a mixture of two or more variants, we have evaluated their individual bioactivities. The variants were resolved by cation exchange HPLC. Bioactivity measurement on murine thymocytes gave a potency order of Ala1 > des-Ala1 > Met0-IL-1β. Analysis using human T-cells co-stimulated with PMA showed a potency order of Ala1 > des-Ala1 > Met0-IL-1β. Thus changes in the N-terminal amino acid of IL-1β changes the activity of the protein. Since murine and human T-cells respond similarly, the interactions between the N-terminus of rhIL-1β and their receptors probably occur through comparable mechanisms.

DOI: 10.1007/BF01972793

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Cite this paper

@article{Richard2005IsolationAB, title={Isolation and bioactivities of three IL-1β N-terminal variants}, author={Karen A. Richard and Anthony W. Yem and Martin R. Deibel and Nigel D. Staite}, journal={Agents and Actions}, year={2005}, volume={27}, pages={268-270} }