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Bryostatin 1 activates protein kinase C and induces monocytic
differentiation of HL-60 cells
RM Stone, E Sariban, GR Pettit and DW Kufe
Laboratory of Clinical Pharmacology, Dana-Farber Cancer Institute, Boston,
MA 02115.
Phorbol esters induce the human HL-60 promyelocytic cell line to
differentiate along a monocytic pathway. This induction of differentiation
may involve phorbol ester-induced activation of the phospholipid- and
calcium-dependent protein kinase C. Bryostatin 1, a macrocyclic lactone,
has been shown to compete with phorbol esters for binding to protein kinase
C. We have confirmed that bryostatin 1 translocates activity of protein
kinase C from the cytosolic to membrane fractions of HL-60 cells. The
present results also demonstrate that bryostatin 1 (10 nmol/L) induces
monocytic differentiation of HL- 60 cells as determined by adherence,
growth inhibition, appearance of monocyte cell surface antigens, and
alpha-naphthyl acetate esterase staining. Furthermore, bryostatin 1 (10
nmol/L) downregulated c-myc expression and induced c-fos, c-fms, and tumor
necrosis factor transcripts. These changes in gene expression induced by
bryostatin 1 are similar to those associated with phorbol ester-induced
monocytic differentiation of HL-60 cells. In contrast, exposure to a higher
concentration of bryostatin 1 (100 nmol/L) had less of an effect on growth
inhibition of HL-60 cells and changes in gene expression. Moreover, 100
nmol/L bryostatin 1 antagonized the cytostatic effects and adherence
induced by phorbol esters. Our results thus suggest that bryostatin 1
activates HL-60 cell protein kinase C and that this effect is associated
with induction of monocytic differentiation.
Volume 72,
Issue 1,
pp. 208-213,
07/01/1988
Copyright © 1988 by The American Society of Hematology
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