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Modulation of Protein Kinase C- by Phorbol Esters in the Monoblastoid U937 Cell¹

Departments of Medicine and Microbiology/Immunology, East Carolina University, School of Medicine, Greenville, North Carolina 27858-4354 [D. K. W., B. R. M., T. O. G., W. Q., P. P. C.], and Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London, United Kingdom WC2A 3PX [P. J. P.]

Expression of protein kinase C- was examined in the human monoblastoid U937 cell. This cell type contained the , ß, and isoforms of protein kinase C (PKC). While PKC- content was slightly higher in the cytosolic than in the particulate fraction, the amount contained in the particulate fraction was higher than the and ß isoforms which were predominantly localized to the cytosol. After an acute exposure to tetradecanoyl-13-phorbol acetate (TPA), PKC- translocated to the particulate fraction. Acute or chronic exposure to ionomycin did not alter content of the isoform. Longer exposures to TPA decreased PKC- in both cellular fractions. PKC- displayed a similar sensitivity to TPA-induced down-regulation as did PKC-ß while PKC- was more resistant to this effect. After a 72-h exposure to 0.1 nM TPA, increases in the and ß isoforms but not in PKC- were observed. However, 1,25-dihydroxy vitamin D₃ and dibutyryl cyclic AMP which induce U937 differentiation enhanced PKC- expression.

¹ This work was supported by NIH Grant CA43023, a Senior International Fogarty Fellowship, and American Cancer Society Junior Faculty Award JFRA230.

² To whom requests for reprints should be addressed.

Received 9/16/91. Accepted 8/10/92.

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