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J. Biol. Chem., Vol. 265, Issue 1, 63-69, 01, 1990
S Cotecchia, BK Kobilka, KW Daniel, RD Nolan, EY Lapetina, MG Caron, RJ Lefkowitz and JW Regan
The alpha-adrenergic receptors mediate the effects of epinephrine and
norepinephrine on cellular signaling systems via guanine nucleotide binding
regulatory proteins (G-proteins). Three alpha-adrenergic receptor subtypes
have been cloned: the alpha 1, the alpha 2-C10, and the alpha 2-C4
adrenergic receptors. To investigate functional differences between the
different subtypes, we assessed the ability of each to interact with
adenylyl cyclase and polyphosphoinositide metabolism by permanently and
transiently expressing the DNAs encoding the alpha 1, the alpha 2-C10, and
the alpha 2-C4 adrenergic receptors in cells lacking endogenous
alpha-adrenergic receptors. Both alpha 2- C10 and alpha 2-C4 couple
primarily to inhibition of adenylyl cyclase and to a lesser extent to
stimulation of polyphosphoinositide hydrolysis. alpha 2-C10 inhibits
adenylyl cyclase more efficiently than alpha 2-C4. Effects of the alpha
2-adrenergic receptors on adenylyl cyclase inhibition and on
polyphosphoinositide hydrolysis are both mediated by pertussis
toxin-sensitive G-proteins. The major coupling system of the alpha
1-adrenergic receptor is activation of phospholipase C via a pertussis
toxin-insensitive G-protein. alpha 1- Adrenergic receptor stimulation can
also increase intracellular cAMP by a mechanism that does not involve
direct activation of adenylyl cyclase. As with the muscarinic cholinergic
receptor family our results show that each of the alpha-adrenergic receptor
subtypes can couple to multiple signal transduction pathways and suggest
several generalities about the effector coupling mechanisms of
G-protein-coupled receptors.
Multiple second messenger pathways of alpha-adrenergic receptor subtypes expressed in eukaryotic cells
Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
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