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Originally published In Press as doi:10.1074/jbc.C100195200 on April 30, 2001

J. Biol. Chem., Vol. 276, Issue 24, 20827-20830, June 15, 2001
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ACCELERATED PUBLICATION
Cyclic AMP-independent Activation of Protein Kinase A by Vasoactive Peptides*

Nickolai O. DulinDagger , Jiaxin Niu, Darren D. Browning, Richard D. Ye, and Tatyana Voyno-Yasenetskaya

From the Department of Pharmacology, University of Illinois at Chicago College of Medicine, Chicago, Illinois 60612

Protein kinase A (PKA) is an important effector enzyme commonly activated by cAMP. The present study focuses on our finding that the vasoactive peptide endothelin-1 (ET1), whose signaling is not coupled to cAMP production, stimulates PKA in two independent cellular models. Using an in vivo assay for PKA activity, we found that ET1 stimulated PKA in HeLa cells overexpressing ET1 receptors and in aortic smooth muscle cells expressing endogenous levels of ET1 receptors. In these cell models, ET1 did not stimulate cAMP production, indicating a novel mechanism for PKA activation. The ET1-induced activation of PKA was found to be dependent on the degradation of inhibitor of kappa B, which was previously reported to bind and inhibit PKA. ET1 potently stimulated the nuclear factor-kappa B pathway, and this effect was inhibited by overexpression of the inhibitor of kappa B dominant negative mutant (Ikappa Balpha m) and by treatment with the proteasome inhibitor MG-132. Importantly, Ikappa Balpha m and MG-132 had similar inhibitory effects on ET1-induced activation of PKA without affecting Gs-mediated activation of PKA or ET1-induced phosphorylation of mitogen-activated protein kinase. Finally, another vasoactive peptide, angiotensin II, also stimulated PKA in a cAMP-independent manner in aortic smooth muscle cells. These findings suggest that cAMP-independent activation of PKA might be a general response to vasoactive peptides.

* This work was supported by National Institutes of Health Grant GM56159 and a grant from American Heart Association (to T. V. Y.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Pharmacology (M/C 868), Medical Sciences Bldg., Rm. E-407, 835 S. Wolcott Ave., University of Illinois at Chicago, Chicago, IL 60612. Tel.: 312-355-2568; Fax: 312-996-1225; E-mail: dulin@uic.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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