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Originally published In Press as doi:10.1074/jbc.M910471199 on April 17, 2000

J. Biol. Chem., Vol. 275, Issue 25, 19395-19400, June 23, 2000
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p38 Mitogen-activated Protein Kinase Pathway Protects Adult Rat Ventricular Myocytes against beta -Adrenergic Receptor-stimulated Apoptosis
EVIDENCE FOR Gi-DEPENDENT ACTIVATION*

Catherine Communal, Wilson S. Colucci, and Krishna SinghDagger

From the Myocardial Biology Unit and Cardiovascular Division, Boston University Medical Center, Boston Veterans Affairs Medical Center and Boston University School of Medicine, Massachusetts 02118

We have shown that stimulation of beta -adrenergic receptors (beta -AR) by norepinephrine (NE) increases apoptosis in adult rat ventricular myocytes (ARVMs) via a cAMP-dependent mechanism that is antagonized by activation of Gi protein. The family of mitogen-activated protein kinases (MAPKs) is involved in the regulation of cardiac myocyte growth and apoptosis. Here we show that beta -AR stimulation activates p38 kinase, c-jun N-terminal kinases (JNKs), and extracellular signal-regulated kinase (ERK1/2) in ARVMs. Inhibition of p38 kinase with SB-202190 (10 µM) potentiated beta -AR-stimulated apoptosis as measured by flow cytometry and terminal deoxynucleotidyl transferase-mediated nick end labeling (TUNEL) staining. SB-202190 at this concentration specifically blocked beta -AR-stimulated activation of p38 kinase and its downstream substrate MAPK-activated protein kinase-2 (MAPKAPK2). Pertussis toxin, an inhibitor of Gi/Go proteins, blocked the activation of p38 kinase and potentiated beta -AR-stimulated apoptosis. Activation of Gi protein with the muscarinic receptor agonist carbachol protected against beta -AR-stimulated apoptosis. Carbachol also activated p38 kinase, and the protective effect of carbachol was abolished by SB-202190. PD-98059 (10 µM), an inhibitor of ERK1/2 pathway, blocked beta -AR-stimulated activation of ERK1/2 but had no effect on apoptosis. These data suggest that 1) beta -AR stimulation activates p38 kinase, JNKs, and ERK1/2; 2) activation of p38 kinase plays a protective role in beta -AR-stimulated apoptosis in cardiac myocytes; and 3) the protective effects of Gi are mediated via the activation of p38 kinase.

* Supported by Grants HL-057947 (to K. S.), HL-42539 and HL-61639 (to W. S. C.); a grant-in-aid from the American Heart Association (AHA), New England Affiliate (to K. S.); a Merit grant from the Department of Veterans Affairs (to K. S.); and a fellowship from the AHA, Massachusetts Affiliate (to C. C.).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: Boston University Medical Ctr., 80 E. Concord St., Boston, MA 02118. Tel.: 617-638-8072; Fax: 617-638-8081; E-mail: krishna.singh@bmc.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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