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The Journal of Immunology, 1998, 160: 2207-2214.
Copyright © 1998 by The American Association of Immunologists

Different Protein Kinase C Isoenzymes Regulate IL-2 Receptor Expression or IL-2 Synthesis in Human Lymphocytes Stimulated via the TCR1

Marta Szamel2,*, Annette Appel*, Reinhard Schwinzer{dagger} and Klaus Resch*

* Institute of Molecular Pharmacology and {dagger} Transplantation Laboratory, Medical School, Hannover, Germany

Stimulation of purified human PBL with mAbs raised against the T cell receptor resulted in an immediate and transient activation of protein kinase C-{alpha} (PKC-{alpha}) and PKC-{theta}, peaking at 10 min, whereas PKC-ß, -{delta}, and -{epsilon} were translocated with a delay of >90 min and remained activated for up to 2 h. To characterize specific functions of distinct PKC isoenzymes, Abs against different PKC isoenzymes were introduced by means of electropermeabilization. Neutralization of PKC-{alpha} and -{theta} resulted in the complete inhibition of IL-2R expression, whereas anti-PKC-ß, -{delta}, and -{epsilon} Abs inhibited IL-2 synthesis. Extensive control experiments have shown that neither electropermeabilization nor control Ig influenced PKC activity and cellular functions. Our data thus clearly show that specific PKC isoenzymes regulate different cellular functions in stimulated human lymphocytes.




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