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Protein Kinase C Activities with Different Characteristics, Including Substrate Specificity, from Two Human HL-60 Leukemia Cell Variants¹

Division of Biological, Environmental, and Medical Research, Argonne National Laboratory, Argonne, Illinois 60439-4833

To evaluate the role of protein kinase C in the cellular maturation processes induced by phorbol diesters, we examined the biochemical activity of protein kinase C from HL-205, a cell variant from the human promyelocytic HL-60 leukemia that is susceptible to differentiation induced by phorbol 12-myristate 13-acetate, and from HL-525, an HL-60 variant that is resistant to such an induction. The activities of protein kinase C from the two cell types differed in their requirements for the cofactors Ca²⁺ and lipids. These enzyme activities also differed in their abilities to phosphorylate protamine and a series of four oligopeptides. We suggest that the differences in vitro in the activities of protein kinase C between HL-205 and HL-525 cells, especially in their substrate specificity, are closely related to the different phosphorylation patterns induced in vivo by phorbol 12-myristate 13-acetate in these cells. We also suggest that these differences may be responsible for the different susceptibilities of the two cell types to maturation induced by phorbol diesters.

¹ This investigation was supported by the U. S. Department of Energy under contract W-31-109-ENG-38.

² To whom requests for reprints should be addressed.

Received 10/26/87. Revised 2/ 9/88. Accepted 2/15/88.

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