Abstract
Although activated human T and B lymphocytes express both high-affinity and low-affinity membrane receptors for interleukin-2 (IL-2)1–3, the structural features that distinguish these receptors have remained unresolved. The high-affinity receptors appear to mediate IL-2 induced T cell growth1,2 and internalization of IL-24,5, whereas no function has yet been ascribed to the low-affinity receptors. The Tac antigen is an IL-2 binding protein6–11 of relative molecular mass 55,000 (Mr 55K) that participates in the formation of both high- and low-affinity receptors2. But Tac complementary DNA transfection12–17 and membrane fusion18 studies have suggested that additional T-cell components are required to produce high-affinity IL-2 receptors. In this study, we report the identification of a second human IL-2 binding protein that (1) has an Mr of ˜70K, (2) lacks reactivity with the anti-Tac antibody, (3) binds IL-2 with intermediate affinity and (4) is present on the surface of resting T cells, large granular lymphocytes (natural killer cells), and certain T and B cell lines in the absence of the Tac antigen. Chemical crosslinking of 125I-labelled IL-2 bound to high-affinity IL-2 receptors produces labelling of both the p70 protein and the Tac antigen and the anti-Tac antibody blocks the crosslink detection of both of these proteins. Expression of Tac cDNA in a T cell line expressing the p70 protein, but lacking both Tac and high-affinity receptors, results in the reconstitution of high-affinity IL-2 receptors in these cells. Together, these findings suggest that the high-affinity human IL-2 receptor may be a membrane complex composed of at least the p70 protein and Tac antigen.
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Dukovich, M., Wano, Y., thi Rich Thuy, L. et al. A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors. Nature 327, 518–522 (1987). https://doi.org/10.1038/327518a0
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DOI: https://doi.org/10.1038/327518a0
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