High level stable expression of human interleukin-2 receptors in mouse cells generates only low affinity interleukin-2 binding sites.
A bovine papilloma virus-derived vector was used to direct the high level expression in mouse C127 cells of three different cDNAs encoding the human interleukin-2 receptor. These were: the previously described cDNA clone isolated from the T-cell lymphoma, HUT-102; a cDNA clone isolated from mitogen-activated, normal peripheral blood T cells; and an altered version of the HUT-102 receptor in which Ser247, believed to be the site of protein kinase C-mediated phosphorylation, has been changed to an Ala residue. Fluorescence-activated cell-sorting using a monoclonal antibody directed against the human IL-2 receptor was used to derive stable lines of C127 cells expressing from 2-6 X 10(6) IL-2 binding sites per cell. However, all of these receptors bound IL-2 with low affinity.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D002460:Cell Line; D004247:DNA / Q000302:isolation & purification; D006801:Humans; D007376:Interleukin-2 / Q000276:immunology*; D051379:Mice; D011971:Receptors, Immunologic / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D015375:Receptors, Interleukin-2; D014170:Transformation, Genetic
D000911:Antibodies, Monoclonal; D007376:Interleukin-2; D011971:Receptors, Immunologic; D015375:Receptors, Interleukin-2; D004247:DNA