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(Received for publication, July 8, 1996, and in revised form, January 22, 1997)
From the Departments of Experimental Therapeutics and
The molecular mechanisms underlying protein
kinase C (PKC) isozyme-mediated control of cell growth and cell cycle
progression are poorly understood. Our previous analysis of PKC isozyme
regulation in the intestinal epithelium in situ revealed
that multiple members of the PKC family undergo changes in expression
and subcellular distribution precisely as the cells cease proliferating
in the mid-crypt region, suggesting that activation of one or more of these molecules is involved in negative regulation of cell growth in
this system (Saxon, M. L., Zhao, X., and Black, J. D. (1994) J. Cell Biol. 126, 747-763). In the present study, the role of PKC
isozyme(s) in control of intestinal epithelial cell growth and cell
cycle progression was examined directly using the IEC-18 immature crypt
cell line as a model system. Treatment of IEC-18 cells with PKC
agonists resulted in translocation of PKC
Volume 272, Number 14,
Issue of April 4, 1997
pp. 9424-9435
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
and
Molecular Medicine, Roswell Park Cancer Institute,
Buffalo, New York 14263
, 
, and 
from the
soluble to the particulate subcellular fraction, cell cycle arrest in
G1 phase, and delayed transit through S and/or G2/M phases. PKC-mediated cell cycle arrest in
G1 was accompanied by accumulation of the
hypophosphorylated, growth-suppressive form of the retinoblastoma
protein and induction of the cyclin-dependent kinase
inhibitors p21waf1/cip1 and p27kip1. Reversal of these
cell cycle regulatory effects was coincident with activator-induced
down-regulation of PKC , , and . Differential down-regulation
of individual PKC isozymes revealed that PKC in particular is
sufficient to mediate cell cycle arrest by PKC agonists in this system.
Taken together, the data implicate PKC in negative regulation of
intestinal epithelial cell growth both in vitro and
in situ via pathways which involve modulation of Cip/Kip
family cyclin-dependent kinase inhibitors and the
retinoblastoma growth suppressor protein.
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