Phosphorylation of a Mr 70,000 protein is associated with interleukin 2 receptor expression.

摘要: The human T cell hybrid II23 was isolated from fusions between peripheral blood lymphocytes which had been stimulated with phytohemagglutinin (PHA) and a subline of the line CEM called CEM.TET1. This does not constitutively express detectable levels interleukin 2 (IL 2) receptors but can be induced to by stimuli shown activate cells. Antibody CD3 (a component receptor) coupled agarose or PHA (greater than 3 micrograms/ml) both IL production receptor expression on Phorbol 12-myristate 13-acetate (PMA) cells secretion. Because PMA is known activator Ca2+/phospholipid-dependent enzyme protein kinase C, proteins unstimulated were analyzed two-dimensional gel electrophoresis for changes in phosphoprotein patterns. A Mr 70,000 pI 6.2 phosphorylated hybrids PMA, anti-CD3 antibody PHA, i.e. same induce these immunosuppressive drug cyclosporin inhibited release without altering induction phosphorylation protein. 70-kDa located cytosol, where it remained at least 4 h after stimulation. migratory properties gels similarly stimulation normal lymphocytes, indicating that phenomenon due hybridization transformation. 70-kDA may therefore involved pathway leads transcription receptors.