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Cited by 223

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Dual Effect of β-Adrenergic Receptors on Mitogen-activated Protein Kinase

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Crespo, Piero, Cachero, Teresa G., Xu, Ningzhi, Gutkind, J. Silvio·1995·Journal of Biological Chemistry
DOI 10.1074/jbc.270.42.25259
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Abstract

The enzymatic activity of mitogen-activated protein kinases (MAP kinases) increases in response to agents acting on a variety of cell surface receptors, including receptors linked to heterotrimeric G proteins of the Gi and Gq family. Recently, it has been shown that stimulation of beta-adrenergic receptors, which are typical of those that act through Gs to activate adenylyl cyclases, potently activates MAP kinases in the heart, resulting in the hypertrophy of the cardiac muscle (Lazou, A., Bogoyevitch, M.A., Clerk, A., Fuller, S.J., Marshall, C.J., and Sudgen, P.H. (1994) Circ. Res. 75, 938-941). We have observed that exposure of COS-7 cells to a beta-adrenergic agonist, isoproterenol, raises intracellular levels of cAMP and effectively activates protein kinase A (PKA) and an epitope-tagged MAP kinase. However, MAP kinase stimulation by isoproterenol was neither mimicked by expression of an activated mutant of G alpha s, nor by treatment with PKA-stimulating agents. Moreover, pretreatment of COS-7 with a permeable cAMP analog, 8-Br-cAMP, markedly decreased MAP kinase activation by either isoproterenol or epidermal growth factor. Thus, in COS-7 cells cAMP and PKA do not appear to mediate MAP kinase activation by beta-adrenergic receptors. Signaling from beta-adrenergic receptors to MAP kinase was inhibited by transfection of a chimeric molecule consisting of the CD8 receptor and the carboxyl terminus of the beta-adrenergic receptor kinase, which includes the beta gamma-binding domain. MAP kinase activation by isoproterenol was not affected by depletion of protein kinase C, but it was completely abolished by expression of Ras-inhibiting molecules. We conclude that signaling from beta-adrenergic receptors to MAP kinase involves an activating signal mediated by beta gamma subunits acting on a Ras-dependent pathway and a G alpha s-induced inhibitory signal mediated by cAMP and PKA. The balance between these two opposing mechanisms of regulation would be expected to control the MAP kinase response to beta-adrenergic agonists as well as to other biologically active agents known to act on Gs coupled receptors, including a number of hormones, neurotransmitters, and lipid mediators.

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Metadata

Authors
Crespo, P., Cachero, T. G., Xu, N., & Gutkind, J. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-10
Volume
270
Issue
42
Pages
25259-25265
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.270.42.25259
OpenAlex
W2020960374
Cited by
223
References
1
FWCI
6.39
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: Dual Effect of β-Adrenergic Receptors on Mitogen-activated Protein Kinase. https://app.cochat.ai/papers/10.1074/jbc.270.42.25259
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Crespo, P., Cachero, T. G., Xu, N., & Gutkind, J. S. (1995). Dual Effect of β-Adrenergic Receptors on Mitogen-activated Protein Kinase. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.42.25259

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