Role of the C-terminus in the biological activity of human interleukin 5

• Published in: Biochemical and biophysical research communications Vol. 178; no. 2; pp. 514 - 519
• Main Authors: Kodama, Shiho, Tsuruoka, Nobuo, Tsujimoto, Masafumi
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.07.1991; Elsevier
• Subjects: Analysis of the immune response. Humoral and cellular immunity; Animals; Biological and medical sciences; Cell Differentiation - drug effects; Cell Line; Chloramines; Chromatography, High Pressure Liquid; Cyanogen Bromide; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Humans; Immunobiology; Immunoglobulin M - biosynthesis; Indicators and Reagents; Interleukin-5 - genetics; Interleukin-5 - isolation & purification; Interleukin-5 - pharmacology; Lymphokines, interleukins ( function, expression); Oxidation-Reduction; Peptide Fragments - isolation & purification; Peptide Fragments - pharmacology; Recombinant Proteins - isolation & purification; Recombinant Proteins - pharmacology; Regulatory factors and their cellular receptors; Tosyl Compounds; Transfection; Human; Interleukin 5; C terminal peptide; Structure activity relation; Cytokine; Deletion; Oxidation; Recombinant protein; Biological activity
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(91)90137-V

Alterations of the C-terminal amino acid sequence of recombinant human interleukin 5 (rhIL-5) caused significant changes in its biological activity. Removal of eight amino acids from the C-terminus of rhIL-5 by CNBr treatment led to a complete loss of biological activity as determined by the BCL 1 cell IgM-inducing assay. Oxidation of Met residue located at C-terminus also resulted in a loss of activity. These results suggest that the C-terminal amino acids of rhIL-5 are crucial for its biological actions.