אסיף מאגר המחקר החקלאי

The human interleukin 2 receptor β chain (p70). Direct identification, partial purification, and patterns of expression on peripheral blood mononuclear cells

Year:

1988

Source of publication :

Authors :

Volume :

167

Co-Authors:

Sharon, M., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Siegel, J.P., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Tosato, G., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Yodoi, J., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Gerrard, T.L., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States
Leonard, W.J., Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, United States

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Abstract:

IL-2 binds to high- and low-affinity receptors on activated T cells. The high-affinity receptor was hypothesized to consist of the noncovalent association between the α chain (IL-2-R-α, p55) and a β chain (IL-2-R-β, p70), whereas the low-affinity receptor consists of p55 without p70. We now directly identify p70 as a 65-77-kD glycoprotein doublet. Preparative quantities of the IL-2/p70 complex have been isolated. Further, we demonstrate that p70 is the principal IL-2-binding protein on both resting CD4+ and CD8+ T cells and that both p70 and p55 can be induced on normal B cells and monocytes.

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