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J Biol Chem, Vol. 273, Issue 45, 30033-30038, November 6, 1998
1 Adrenergic
Receptors
From the Veterans Affairs Palo Alto Health Care System, Geriatrics,
Research, Education, and Clinical Center,
Palo Alto, California 94304 and Department of Medicine, Stanford
University, School of Medicine, Stanford, California 94305
Activation of 
1 adrenergic
receptors not only stimulates smooth muscle contraction but also
modifies gene expression. We wondered if 1 adrenergic
receptors could activate transcription of genes regulated by the cAMP
response element-binding protein (CREB). Using Rat1 cells stably
transfected with each of the three cloned human 1
adrenergic receptor subtypes, norepinephrine strongly stimulated CREB
phosphorylation in 1A and 1B but more
weakly in 1D-transfected cells. Norepinephrine increased
the activity of a somatostatin cAMP-regulated enhancer-chloramphenicol
acetyltransferase reporter in these cells. 1 adrenergic
receptors are known to activate protein kinase C (PKC) and increase
[Ca2+ ]i. Nonetheless, neither GF109203X, a PKC
inhibitor, nor BAPTA-AM, a calcium chelator, blocked phosphorylation of
CREB induced by norepinephrine. In addition, 1
adrenergic receptor-induced CREB phosphorylation was not mediated via
the mitogen-activated protein kinase pathway because norepinephrine did
not stimulate mitogen-activated protein kinase activity in these cells.
Activation of 1 adrenergic receptors increased cAMP
accumulation in these cells. Norepinephrine-induced cAMP-regulated
enhancer-chloramphenicol acetyltransferase activity was inhibited
either by expression of the PKA inhibitory peptide or a dominant
negative PKA regulatory subunit mutant. These results demonstrate that
1 adrenergic receptors activate the transcription factor
CREB by a PKA-dependent pathway.
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