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J Biol Chem, Vol. 274, Issue 30, 20805-20811, July 23, 1999
Inhibition of S-Phase Transition in
Capillary Endothelial Cells Involves the
Cyclin-dependent Kinase Inhibitor
p27Kip1
§,§,§, and
From the Distinct protein kinase C (PKC) isoforms
differentially regulate cellular proliferation in rat microvascular
endothelial cells (EC). Overexpression of PKC Cardiovascular Division and the Departments
of ** Developmental and Molecular Biology,
Molecular Pharmacology, and
§ Medicine, Albert Einstein College of Medicine, Bronx, New
York 10461
has little effect on
proliferation, whereas PKC
slows endothelial cell proliferation and
induces S-phase arrest. Analyses were performed on EC overexpressing
PKC (PKCEC) or PKC (PKCEC) to determine the role of
specific cell cycle regulatory proteins in the PKC-induced cell
cycle arrest. Serum-induced stimulation of cyclins D1, E, and
A-associated kinase activity was delayed by 12 h in the PKCEC
line in association with S-phase arrest. However, the protein levels
for cyclins D1, E, and A were similar. Nuclear accumulation of cyclin
D1 protein in response to serum was also delayed in PKCEC. In the
PKCEC line, serum induced p27Kip1 but not
p16Ink4a or p21Cip1. Serum did not affect
p27Kip1 levels in the control vascular endothelial cell
line. Immunoprecipitation-Western blotting analysis of
p27Kip1 showed serum stimulation of the vascular
endothelial cell line resulted in increased amounts of cyclin D1 bound
to p27Kip1. In the PKCEC line, serum did not increase
the amount of cyclin D1 bound to p27Kip1. Transfection of
full-length p27Kip1 antisense into the PCKEC line
reversed the S-phase arrest and resulted in normal cell cycle
progression, suggesting a critical role for p27Kip1 in the
PKC-mediated S-phase arrest.
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