A mouse hybridoma cell line, TU27, producing an mAb was established. TU27 mAb reacted with various human and Gibbon ape T cell lines bearing the IL-2R p75 (IL-2Rp75), but not with cell lines expressing only Tac antigen, IL-2Rp55, and numbers of its binding sites on cell surfaces were similar to those of high-affinity IL-2R. Radioimmunoprecipitation with TU27 mAb defined a molecule with a molecular mass of 75 kD on the surface of IL-2Rp75 bearing cells. TU27 mAb completely blocked IL-2 binding to IL-2Rp75 and to the high-affinity IL-2R but not to IL-2Rp55 composing the low-affinity IL-2R. The IL-2-dependent growth of a human T cell line, ILT-Mat, was significantly inhibited by TU27 mAb only at low concentrations of IL-2, and combination of TU27 mAb and H-31 mAb specific for IL-2Rp55 completely inhibited the cell growth even at high concentrations of IL-2. These data strongly suggest that TU27 mAb is specific for the human IL-2Rp75.
Monoclonal antibody defining a molecule possibly identical to the p75 subunit of interleukin 2 receptor.
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T Takeshita, Y Goto, K Tada, K Nagata, H Asao, K Sugamura; Monoclonal antibody defining a molecule possibly identical to the p75 subunit of interleukin 2 receptor.. J Exp Med 1 April 1989; 169 (4): 1323–1332. doi: https://doi.org/10.1084/jem.169.4.1323
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