October 1, 1987The Journal of Immunology
The role of protein kinase C in transmembrane signaling by the T cell antigen receptor complex. Effects of stimulation with soluble or immobilized CD3 antibodies.
Authors
Discussion
Loading...
Member takes
Implication
Experimental study demonstrates that immobilized CD3 antibodies sustain protein kinase C activation in T cells, indicating why physical antibody presentation dictates immune activation.
Key Points
- To determine the role of protein kinase C activation in T-cell receptor transmembrane signaling and evaluate how soluble versus immobilized anti-CD3 antibodies regulate this pathway.
- Stimulated purified human T lymphocytes and Jurkat leukemic T cells with the metabolizable synthetic diacylglycerol, dioctanoylglycerol, alone or alongside calcium ionophores or anti-CD3 monoclonal antibodies.
- Measured interleukin-2 receptor expression and cellular proliferation following stimulation.
- Compared the kinetics of protein kinase C activation in Jurkat cells following challenge with soluble versus plastic-immobilized anti-CD3 monoclonal antibodies.
- Dioctanoylglycerol synergized with calcium ionophores or anti-CD3 monoclonal antibodies to induce robust interleukin-2 receptor expression and proliferation in resting T lymphocytes.
- Soluble anti-CD3 antibodies stimulated only brief, transient activation of protein kinase C in Jurkat cells and failed to trigger resting T-cell proliferation.
- Immobilization of anti-CD3 antibodies converted transient protein kinase C activation into markedly prolonged enzymatic activity, demonstrating that physical presentation controls the duration of intracellular signaling.
Cite This Study
Manger et al. (1987) studied this question.