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Vol. 57, Issue 3, 460-467, March 2000
Department of Medicine, Division of Cardiology, Emory
University, Atlanta, Georgia
The effects of angiotensin II (Ang II) are mediated primarily by
Ang II type 1 receptors, which in turn are coupled to heterotrimeric G
proteins. After receptor activation, the G
and
G
subunits dissociate, contributing to the
signaling cascades involving protein kinase C (PKC) activation.
Regulators of G protein signaling (RGS proteins) comprise a class of
proteins that have been shown to negatively regulate the
G subunit. We examined which RGS sequences were
expressed in vascular smooth muscle cells and which of these were
regulated by Ang II. Reverse transcription-polymerase chain reaction
showed that of 16 RGS sequences screened, six RGS transcripts (RGS2, 3, 10, 11, and 12 and GAIP) were present. Northern blot analysis
demonstrated that RGS3, 10, and 12 and GAIP were not regulated by Ang
II at the mRNA level. In contrast, RGS2 mRNA was rapidly and dose
dependently increased (395 ± 24% peak, 45 min) by Ang II but
returned to baseline level by 6 to 8 h.
Phorbol-12-myristate-13-acetate, a PKC activator, robustly
increased RGS2. This signal was attenuated by the PKC inhibitor GF
109203X (50 ± 4%) and by
phorbol-12,13-dibutyrate-mediated down-regulation of PKC
(48 ± 13%). Tyrosine kinase inhibition and calcium deprivation
did not affect the up-regulation of RGS2 mRNA after Ang II stimulation.
Actinomycin D treatment inhibited both Ang II- and
phorbol-12-myristate-13-acetate-stimulated RGS2 up-regulation,
suggesting activation of transcription by these agonists. The stability
of RGS2 mRNA did not appear to be affected by Ang II. Thus, RGS2 is a
likely candidate for negative regulation of the G proteins coupled to
the Ang II type 1 receptor in vascular smooth muscle cells. Regulation
of this protein may be of critical importance in modulating the role of
Ang II in vascular disease.
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