Interleukin 2 and a lactogen regulate proliferation and protein phosphorylation in Nb2 cells.

Abstract

Cell proliferation and protein phosphorylation in response to activation of lactogenic and interleukin 2 (IL-2) receptors were studied in Nb2 cells, a rat T-lymphocyte cell line. Human growth hormone (hGH) and rat IL-2 stimulated Nb2-cell proliferation to approximately the same degree, and the actions of both mitogens were potentiated by phorbol 12-myristate 13-acetate (PMA). A monoclonal antibody specific for the rat IL-2 receptor inhibited the mitogenic actions of rat IL-2, but not those of hGH. Exposure of Nb2 cells to either mitogen for 2-3 h increased phosphorylation of an 18,600-Da protein and decreased phosphorylation of a 15,600-Da protein. PMA also inhibited phosphorylation of the latter protein, but, by itself, PMA did not stimulate phosphorylation of the 18,600-Da protein. Overall, the results suggest that hGH and IL-2 act through separate receptors to stimulate proliferation of Nb2 cells, and that some of the actions of both mitogens may be mediated, in part, through regulation of protein phosphorylation.