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J. Biol. Chem., Vol. 276, Issue 10, 7351-7356, March 9, 2001

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Interleukin-2 Carbohydrate Recognition Modulates CTLL-2 Cell Proliferation^*

Keiko Fukushima and Katsuko Yamashita

From the Department of Biochemistry, Sasaki Institute, 2-2 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062 and CREST (Core Research for Evolutional Science and Technology) of the Japan Science and Technology Corporation, 2-3 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062 Japan

Interleukin-2 (IL-2) specifically recognizes high-mannose type glycans with five or six mannosyl residues. To determine whether the carbohydrate recognition activity of IL-2 contributes to its physiological activity, the inhibitory effects of high-mannose type glycans on IL-2-dependent CTLL-2 cell proliferation were investigated. Man₅GlcNAc₂Asn added to CTLL-2 cell cultures inhibited not only phosphorylation of tyrosine kinases but also IL-2-dependent cell proliferation. We found that a complex of IL-2, IL-2 receptor , ,  subunits, and tyrosine kinases was formed in rhIL-2-stimulated CTLL-2 cells. Among the components of this complex, only the IL-2 receptor  subunit was stained with Galanthus nivalis agglutinin which specifically recognizes high-mannose type glycans. This staining was diminished after digestion of the glycans with endo--N-acetylglucosaminidase H or D, suggesting that at least a N-glycan containing Man₅GlcNAc₂ is linked to the extracellular portion of the IL-2 receptor  subunit. Our findings indicate that IL-2 binds the IL-2 receptor  subunit through Man₅GlcNAc₂ and a specific peptide sequence on the surface of CTLL-2 cells. When IL-2 binds to the IL-2R subunit, this may trigger formation of the high affinity complex of IL-2-IL-2R, -, and - subunits, leading to cellular signaling.

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