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T cell activation: distinct pathways involve phosphorylation of different cellular proteins

1988; Wiley; Volume: 18; Issue: 7 Linguagem: Inglês

10.1002/eji.1830180727

1521-4141

Jean‐François Peyron, Suzanne Pont, Michel Pierres, Max Fehlmann,

Glycosylation and Glycoproteins Research

Abstract The murine T cell clone D10.G4.1 can be induced to proliferate by monoclonal antibodies (mAb) to the T cell receptor (TcR) or to Thy‐1 molecules. When cells were stimulated by anti‐TcR mAb, a group of 4 proteins (19–25 kDa) was specifically phosphorylated. This effect was completely mimicked by the Ca 2+ ionophore A23187, whereas only two of these proteins (19 kDa and 25 kDa) were phosphorylated after cell exposure to the phorbol ester 12‐O‐tetradecanoylphorbol 13‐acetate. By contrast, anti‐Thy‐1 mAb had no effect on the phosphorylation of these proteins, but induced specifically the phosphorylation of a protein of 32 kDa. These results therefore demonstrate that distinct activating pathways in T cells involve the phosphorylation of different proteins, suggesting that the stimulation of protein kinases in T lymphocytes is an early event in cell activation.