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Am J Physiol Cell Physiol 283: C1025-C1032, 2002. First published May 29, 2002; doi:10.1152/ajpcell.00096.2002
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Vol. 283, Issue 4, C1025-C1032, October 2002

Duality of G protein-coupled mechanisms for beta -adrenergic activation of NKCC activity in skeletal muscle

Aidar R. Gosmanov, Jennifer A. Wong, and Donald B. Thomason

Department of Physiology, College of Medicine, University of Tennessee Health Science Center, Memphis, Tennessee 38163

Skeletal muscle Na+-K+-2Cl- cotransporter (NKCC) activity provides a potential mechanism for regulated K+ uptake. beta -Adrenergic receptor (beta -AR) activation stimulates skeletal muscle NKCC activity in a MAPK pathway-dependent manner. We examined potential G protein-coupled pathways for beta -AR-stimulated NKCC activity. Inhibition of Gs-coupled PKA blocked isoproterenol-stimulated NKCC activity in both the slow-twitch soleus muscle and the fast-twitch plantaris muscle. However, the PKA-activating agents cholera toxin, forskolin, and 8-bromo-cAMP (8-BrcAMP) were not sufficient to activate NKCC in the plantaris and partially stimulated NKCC activity in the soleus. Isoproterenol-stimulated NKCC activity in the soleus was abolished by pretreatment with pertussis toxin (PTX), indicating a Gi-coupled mechanism. PTX did not affect the 8-BrcAMP-stimulated NKCC activity. PTX treatment also precluded the isoproterenol-mediated ERK1/2 MAPK phosphorylation in the soleus, consistent with NKCC's MAPK dependency. Inhibition of isoproterenol-stimulated ERK activity by PTX treatment was associated with an increase in Akt activation and phosphorylation of Raf-1 on the inhibitory residue Ser259. These results demonstrate a novel, muscle phenotype-dependent mechanism for beta -AR-mediated NKCC activation that involves both Gs and Gi protein-coupled mechanisms.

potassium; mitogen-activated protein kinases; protein kinase A; pertussis toxin; Raf-1


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