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 alpha chain (IL-2-R-alpha, p55) and a beta chain (IL-2-R-beta, 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.
MeSH terms
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Antigens, Surface / genetics
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Antigens, Surface / isolation & purification*
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B-Lymphocytes / analysis
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Gene Expression Regulation
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Glycoproteins / genetics
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Humans
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Interleukin-2 / metabolism*
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Leukocytes, Mononuclear / analysis*
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Leukocytes, Mononuclear / classification
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Lymphocyte Activation
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Molecular Weight
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Receptors, Immunologic / genetics
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Receptors, Immunologic / isolation & purification*
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Receptors, Interleukin-2
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T-Lymphocytes / analysis
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T-Lymphocytes / classification
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Tumor Cells, Cultured
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Tumor Necrosis Factor Receptor Superfamily, Member 7
Substances
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Antigens, Surface
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Glycoproteins
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Interleukin-2
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Receptors, Immunologic
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Receptors, Interleukin-2
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Tumor Necrosis Factor Receptor Superfamily, Member 7