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Activation of protein kinase Cdelta in human myeloid leukemia cells treated
with 1-beta-D-arabinofuranosylcytosine
Y Emoto, H Kisaki, Y Manome, S Kharbanda and D Kufe
Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard
Medical School, Boston, MA, USA.
Treatment of human myeloid leukemia cells with 1-beta-D-
arabinofuranosylcytosine (ara-C) is associated with induction of protein
kinase activity and early-response gene expression. The present studies in
ara-C-treated U-937 cells extend these findings by demonstrating activation
of a protein kinase that phosphorylates myelin basic protein (MBP).
Purification by sequential ion-exchange chromatography and gel filtration
supports the detection of a 40-kD MBP kinase. Substrate and inhibitor
studies further support a pattern similar to that of protein kinase C (PKC)
isozymes. Results of N- terminal amino acid sequencing and immunoblot
analysis demonstrate detection of a 40-kD catalytic fragment of PKCdelta.
The results also demonstrate the activation and cleavage of PKCdelta (1) is
inhibited by expression of antiapoptotic proteins, and (2) is induced by
camptothecin (CAM) and mitomycin C (MMC). These findings support
proteolytic activation of PKCdelta in the cellular response to ara-C and
other DNA-damaging agents.
Volume 87,
Issue 5,
pp. 1990-1996,
03/01/1996
Copyright © 1996 by The American Society of Hematology
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