Characterization of human interleukin 2 receptor (Tac antigen) in normal and leukemic T cells: co-expression of normal and aberrant receptors on Hut-102 cells.

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Abstract
Human interleukin 2 receptors ( IL2R ) from various cell sources such as mitogen-activated normal human T cells, adult T cell leukemia (ATL)-derived cell line cells (MT-1, ATL-6, Hut-102), and a natural killer-like cell line YT cells, were studied both by one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with a monoclonal anti- IL2R antibody (anti-Tac). In synthetic labeling with [35S]methionine, anti-Tac specifically precipitated two glycoproteins, one with m.w. of 60,000 to 65,000 and pI 4.2 to 4.7, and the other with m.w. about 40,000 and pI 6.2 to 6.5. A study of surface iodination revealed that the former component was membrane-associated mature IL2R , and a pulse-chase study showed that the latter component was a precursor for IL2R that already possessed tunicamycin-sensitive N-linked sugar side chain(s). This precursor was found to be posttranslationally processed into mature IL2R by further glycosylation within 240 min. Among the cells studied, a human T cell leukemia virus-positive leukemic cell line, Hut-102, was distinctive in that it possessed an additional membrane glycoprotein (m.w. 55,000 to 60,000, pI 4.2 to 5.0) also defined by anti-Tac. This unique glycoprotein of Hut-102 cells appeared to be an aberrant IL2R .

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