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J. Biol. Chem., Vol. 278, Issue 11, 9472-9480, March 14, 2003
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From INSERM U-533, Faculté des Sciences,
44322 Nantes Cedex 3, France
The small G protein RhoA is a convergence point
for multiple signals that regulate smooth muscle cell functions. NO
plays a major role in the structure and function of the normal adult vessel wall, mainly through modulation of gene transcription. This
study was thus performed to analyze in vitro and in
vivo the effect of NO signaling on RhoA expression in arterial
smooth muscle cells. In rat or human artery smooth muscle cells, sodium nitroprusside or 8-(2-chlorophenylthio)-cGMP induced a rise in RhoA mRNA and protein expression, which was inhibited by the
cGMP-dependent protein kinase (PKG) inhibitor
(Rp)-8-bromo-
RhoA Expression Is Controlled by Nitric Oxide through
cGMP-dependent Protein Kinase Activation*
,§,
-phenyl-1,N2-ethenoguanosine
3':5'-phosphorothioate. The NO/PKG stimulation of RhoA expression
involved both an increase in RhoA protein stability and stimulation of
rhoA gene transcription. Cloning and functional analysis of
the human rhoA promoter revealed that the effect of NO/PKG
involved phosphorylation of ATF-1 and subsequent binding to the
cAMP-response element. Chronic inhibition of NO synthesis in
N
-nitro-L-arginine-treated rats
induced a strong decrease in RhoA mRNA and protein expression in
aorta and pulmonary artery associated with inhibition of RhoA-mediated
Ca2+ sensitization. These effects were prevented by oral
administration of the cGMP phosphodiesterase inhibitor sildenafil.
These results show that NO/PKG signaling positively controls RhoA
expression and suggest that the basal release of NO is necessary to
maintain RhoA expression and RhoA-dependent functions in
vascular smooth muscle cells.
*
This work was supported in part by grants from INSERM,
Institut International de Recherche Servier, Région Pays de
Loire, and Action Cibles Thérapeutiques et Médicaments
(INSERM-CNRS).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Both authors contributed equally to this work.
§
Supported by a grant from the Association pour la Recherche contre
le Cancer.
¶
To whom correspondence should be addressed: Laboratoire de
Physiologie Cellulaire et Moléculaire, INSERM U-533,
Faculté des Sciences, 2 rue de la Houssinière, BP 92208, 44322 Nantes Cedex 3, France. Tel.: 33-2-5112-5740; Fax:
33-2-5112-5614; E-mail: pacaud@svt.univ-nantes.fr and
gervaise.loirand{at}nantes.inserm.fr.
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