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Translocation and Activation of Protein Kinase C by the Plasma Cell Tumor-promoting Alkane Pristane

Laboratory of Genetics, National Cancer Institute [S. J.], and Laboratory of Membrane Biochemistry and Biophysics, National Institute of Alcohol Abuse and Alcoholism [K. G.], NIH, Bethesda, Maryland 20892, and Division of Research and Testing, Center for Drug Evaluation and Research, Food and Drug Administration, Laurel, Maryland 20708 [D. S. L.]

Pristane (2,6,10,14-tetramethylpentadecane) is a C₁₉-isolakane that promotes the development of plasmacytomas in genetically susceptible BALB/c mice. Similarities between the effects of pristane and protein kinase C (PKC)-activating phorbol esters suggested that the tumor promoting activity of pristane might involve the activation of PKC. Here we show that up to 5 mol% of pristane can be homogeneously incorporated into phosphatidylcholine/phosphatidylserine bilayers. Membrane-incorporated pristane partially activated PKC and increased phorbol ester binding to the bilayer by more than 50%. Pristane (50 µM) delivered as an inclusion complex with ß-cyclodextrin to promyelocytic HL-60 leukemia cells induced a partial long-term translocation of PKC to the cell membrane. This was accompanied by differentiation of HL-60 cells into macrophage-like cells. It is concluded that activation of PKC may comprise an important aspect of the tumor promoting potential of pristane.

¹ To whom requests for reprints should be addressed, at Laboratory of Genetics, National Cancer Institute/NIH, Building 37, Room 2B09, Bethesda, MD 20892-4255.

Received 8/ 3/94. Accepted 11/30/94.

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