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The Journal of Immunology, Vol 156, Issue 11 4167-4173, Copyright © 1996 by American Association of Immunologists

ARTICLES

Inhibition of constitutive serine phosphatase activity in T lymphoma cells results in phosphorylation of pp19/cofilin and induces apoptosis

Y Samstag, EM Dreizler, A Ambach, G Sczakiel and SC Meuer
Institute for Immunology, Ruprecht-Karls-University, Heidelberg, Germany.

In untransformed T lymphocytes, pp19/cofilin, a cytoplasmic actin- binding protein, undergoes dephosphorylation and nuclear translocation in response to costimulation through accessory receptors (e.g., CD2), but not following TCR/CD3 triggering. In malignant T lymphoma cells, dephosphorylation and nuclear translocation of pp19/cofilin occur spontaneously through constitutive activation of a serine phosphatase. Blockade of these processes by the serine phosphatase inhibitor okadaic acid leads to apoptosis. Moreover, lowering the intracellular pp19/cofilin concentrations by antisense-cofilin transfection results in reduced cloning efficiencies. These findings provide support for the view that pp19/cofilin plays a critical role in the growth and survival of both untransformed and malignant T lymphocytes.


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