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Originally published In Press as doi:10.1074/jbc.M205616200 on November 21, 2002

J. Biol. Chem., Vol. 278, Issue 6, 3969-3975, February 7, 2003
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Endothelin-1-specific Activation of B-type Natriuretic Peptide Gene via p38 Mitogen-activated Protein Kinase and Nuclear ETS Factors*

Sampsa PikkarainenDagger , Heikki TokolaDagger , Risto KerkeläDagger , Theresa Majalahti-Palviainen§, Olli Vuolteenaho§, and Heikki RuskoahoDagger

From the Dagger  Department of Pharmacology and Toxicology and § Department of Physiology, Biocenter Oulu, University of Oulu, P. O. Box 5000, Oulu FIN-90014, Finland

Terminally differentiated cardiac myocytes adapt to mechanical and neurohumoral stress via morphological changes of individual cells accompanied by reactivation of fetal pattern of gene expression. Endothelin-1, a powerful paracrine mediator of myocyte growth, induces similar changes in cultured cardiac myocytes as those seen in hypertrophied heart in vivo. By using rat B-type natriuretic peptide promoter, we identified a novel ETS binding sequence, on which nuclear protein binding is activated in endothelin-1-treated cultured cardiac myocytes. This sequence binds ETS-like gene-1 transcription factor and mediates endothelin-1-specific activation of transcription, but not responses to increased calcium signaling via L-type calcium channels, angiotensin II treatment, or mechanical stretch of myocytes. Interestingly, endothelin-1 activated signaling converges via p38 mitogen-activated protein kinase-dependent mechanism on ETS binding site, whereas this element inhibits extracellular signal-regulated kinase activated transcription. In conclusion, given the fundamental role of the interaction of mitogen-activated protein kinases and ETS factors in regulation of eukaryotic cell differentiation, growth, and oncogenesis, these results provide the unique evidence of a endothelin-1- and mitogen-activated protein kinase-regulated ETS factor pathway for cardiac myocytes.

* This work was supported by grants from the Academy of Finland (to H. R.), the AstraZeneca Research Foundation (to S. P.), the Sigrid Juselius Foundation (to H. R.), the Aarne Koskelo Foundation (to R. K., T. M.-P., and S. P.), the Ida Montin Foundation (to R. K. and S. P.), the Finnish Foundation for Cardiovascular Research (to H. R., S. P., and R. K.), the Research Foundation of Orion Co. (to R. K.), and the Finnish Cultural Foundation (to S. P.).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.

To whom correspondence should be addressed. Tel.: 358-8-537-5236; Fax: 358-8-537-5247; E-mail: heikki.ruskoaho@oulu.fi.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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