Oct 15, 1989

The beta-chain of the IL-2 receptor (p70) is tyrosine-phosphorylated on YT and HUT-102B2 cells

The Journal of Immunology : Official Journal of the American Association of Immunologists
M SharonW J Leonard


IL-2 has previously been shown to rapidly induce activity of a tyrosine kinase. High-affinity IL-2 receptors that mediate the major mitogenic signals of IL-2 contain both p70 and p55 chains. p55 has no potential tyrosine phosphorylation sites and lacks consensus sequences found in protein tyrosine kinases. Inasmuch as the phosphorylation of hormone receptors is generally an important mechanism for regulating receptor function, we have now investigated the phosphorylation status of p70. By using anti-phosphotyrosine antibodies to immunoprecipitate affinity-labeled IL-2 receptors and to probe Western blots, we provide data suggesting that p70, but not p55, is constitutively tyrosine-phosphorylated on the leukemic cell lines studied.

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Mentioned in this Paper

Precipitin Tests
Immunoblotting, Reverse
Interleukin 2 Receptor, Alpha
Protein Phosphorylation
Hormone Receptor
Hairy Cell Leukemia
Western Blot
Leukemic Cell

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