Abstract
Publisher Summary This chapter focuses on carbohydrate-binding specificity of interleukin-2 (IL-2) in relation to T-cell proliferation. IL-2 has been widely studied as a mediator of cellular signaling in the immune system. IL-2 promotes the proliferation of IL-2-dependent T cells, and functions as an immunomodulator of activated B cells, macrophages, and natural-killer cells. IL-2 expresses its physiological functions through interaction with its receptor complex, which consists of three receptor subunits:α, β, and γ (IL-2Rα, IL2Rβ, and IL-2Rγ). The chapter discusses the preparation of IL-2, cell proliferation assay, bioassay of rhIL-2, preparation of oligosaccharides, and solid-phase-binding assay. Inhibitory effects of various high mannose-type glycans on IL-2 binding to ribonuclease B are investigated using the plate method. To clarify whether the carbohydrate recognition ability is indispensable for induction of IL-2-dependent cell proliferation, inhibitory effects of high mannose-type glycans on CTLL-2 cell proliferation are investigated. Inhibition of [35S]rh IL-2 binding to plates coated with ribonuclease B by oligomannosyl derivatives is also tabulated in the chapter.
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