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Volume 272, Number 50, Issue of December 12, 1997 pp. 31251-31257
Is Required for Mechano-sensitive Activation of
ERK1/2 in Endothelial Cells
(Received for publication, May 22, 1997, and in revised form, August 27, 1997)
,
From the Mechano-sensitive regulation
of endothelial cells (EC) function by shear stress is critical for
flow-induced vasodilation and gene expression. Previous studies by our
laboratory demonstrated that shear stress activates the 44- and 42-kDa
extracellular signal-regulated kinases (ERK1/2) in EC in a time- and
force-dependent manner. ERK1/2 activation was inhibited by
protein kinase C (PKC) down-regulation with phorbol 12,13-dibutyrate (1 µM for 24 h) but not by calcium chelation with
BAPTA-AM (acetoxymethyl ester of BAPTA) (75 µM for 30 min), suggesting that a novel PKC isoform (
Department of Pathology and Department of
Medicine, Division of Cardiology, University of Washington, Seattle,
Washington 98195 and § Department of Molecular Pharmacology,
ISIS Pharmaceuticals, Carlsbad, California 92008
, 
, 
, 
) mediates
shear stress-induced ERK1/2 activation. Western blotting with PKC
isoform-specific antibodies demonstrated expression of PKC-
, -,
and -
isoforms in EC. PKC- was specifically inhibited by
transfection with antisense PKC- phosphorothioate oligonucleotides (1,000 nM for 6 h). Antisense treatment decreased
PKC- protein levels by 80 ± 13% after 72 h and
completely inhibited shear stress-stimulated ERK1/2 activation.
Scrambled PKC- oligonucleotides and antisense PKC- and PKC-
oligonucleotides had no effect on ERK1/2 activity. PKC- appeared
specific for mechano-sensitive ERK1/2 activation, as antisense PKC-
oligonucleotides did not inhibit ERK1/2 activation by EGF or bradykinin
but did inhibit ERK1/2 activation upon EC adhesion to fibronectin.
These results define a pathway for shear stress-mediated ERK1/2
activation and establish a new function for PKC- as part of a
mechano-sensitive signal transduction pathway in EC.
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