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J. Biol. Chem., Vol. 265, Issue 25, 14784-14790, 09, 1990
JR Hadcock, M Ros, DC Watkins and CC Malbon
The hormone-sensitive adenylyl cyclase system is under dual control,
receiving both stimulatory and inhibitory inputs. Guanine nucleotide-
binding regulatory proteins (G-proteins) transduce signals from cell
surface receptors to effectors such as adenylyl cyclase. Hormonal
stimulation is propagated via Gs, inhibition by Gi. Persistent (24-h)
activation of the stimulatory pathway of adenylyl cyclase by the diterpene
forskolin or the beta-adrenergic agonist isoproterenol in S49 mouse
lymphoma cells enhanced the effects of somatostatin mediated via the
inhibitory pathway of adenylyl cyclase. Stimulating cells with forskolin or
isoproterenol for 24 h resulted in a 3-fold increase in the steady-state
levels of Gi alpha 2 and a 25% decline in Gs alpha, as quantified by
immunoblotting. Within 12 h of stimulation of adenylyl cyclase, Gi alpha 2
mRNA levels increased 4-fold, measured by DNA- excess solution
hybridization. Gs alpha mRNA levels, in contrast, increased initially
(25%), but then declined to 75% of control. In S49 variants that lack
functional protein kinase A (kin-), stimulation by isoproterenol failed to
alter Gi alpha 2 expression at either the protein or the mRNA levels. A
3-fold increase in relative synthesis rate and no change in the half-life
(approximately 80 h) of Gi alpha 2 was observed in response to forskolin
stimulation. Although Gs alpha synthesis increased (70%) modestly in
response to forskolin stimulation, the half-life of Gs alpha actually
decreased from 55 h in naive cells to 34 h in treated cells. Thus, the two
G-protein-mediated pathways controlling adenylyl cyclase display
"cross-regulation." Persistent activation of the stimulatory pathway
increases Gi alpha 2 mRNA and expression. Transiently elevated Gs alpha
mRNA levels are counterbalanced by a reduction in the half-life of the
protein.
Cross-regulation between G-protein-mediated pathways. Stimulation of adenylyl cyclase increases expression of the inhibitory G-protein, Gi alpha 2
Department of Pharmacology, School of Medicine, State University of New York, Stony Brook 11794-8651.
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