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Vol. 63, Issue 3, 478-488, March 2003
12,
G13, Gq, and G
for
Endothelin-1-Induced c-Jun NH2-Terminal Kinase and
Extracellular Signal-Regulated Kinase Activation
Laboratory of Pharmacology and Toxicology, Graduate School
of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan (K.A.,
Y.M., M.N., S.Tan., S.Tak., T.N., H.K.); Division of Molecular and
Cellular Physiology, Center for Integrative Bioscience, National
Institute for Physiological Sciences, Okazaki, Japan (M.N., Y.,M.); and
Department of Pharmacology, University of Illinois at Chicago, Chicago,
Illinois (T.K.)
In the present study, we examined the roles of G12,
G13, Gq, and Gi in
endothelin-1-induced hypertrophic responses. Endothelin-1 stimulation
activated extracellular signal-regulated kinase (ERK) and c-Jun
NH2-terminal kinase (JNK) in cultured rat neonatal
myocytes. The activation of JNK, but not ERK, was inhibited by the
expression of carboxyl terminal regions of G
12 and
G13. JNK activation was also inhibited by expression of
the G12/G13-specific inhibitor regulator
of G protein signaling (RGS) domain of p115RhoGEF and the
Gq-specific inhibitor RGS domain of the G
protein-coupled receptor kinase 2 (GRK2-RGS). JNK activation was not,
however, inhibited by expression of the carboxyl terminal region of G
protein-coupled receptor kinase 2 (GRK2-ct), which is a
G
-sequestering polypeptide. Additionally, JNK activation but not
ERK activation was inhibited by the expression of C3 exoenzyme that
inactivates small GTPase Rho. These results suggest that JNK activation
by G12, G13, and Gq is
involved in Rho. On the other hand, ERK activation was inhibited by
pertussis toxin treatment, the receptor-Gi uncoupler, and
GRK2-ct. Thus, ERK was activated by Gi- and
G-dependent pathways. These results clearly demonstrate that
differential pathways activate JNK and ERK.
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