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J Biol Chem, Vol. 274, Issue 33, 22985-22992, August 13, 1999
From the Department of Biochemistry, University of Alberta,
Edmonton, Alberta T6G 2H7, Canada
We examined regulation of the
Na+/H+ exchanger isoform 1 by
phosphorylation in the rat myocardium. We utilized cell extracts from
adult rat hearts, adult rat extracts fractionated by fast performance
liquid chromatography, and extracts from cultured neonatal cardiac
myocytes. The carboxyl-terminal 178 amino acids of the
Na+/H+ exchanger were expressed in
Escherichia coli fused with glutathione S-transferase. The purified protein was used as a substrate
for in vitro phosphorylation and in-gel kinase assays.
Unfractionated extracts from neonatal myocytes or adult hearts
phosphorylated the COOH-terminal domain of the antiporter. Western blot
analysis revealed that mitogen-activated protein (MAP) kinase (44 and
42 kDa) and p90rsk (90 kDa) were present in specific fractions
of cardiac extracts that phosphorylated the COOH-terminal protein.
In-gel kinase assays confirmed that protein kinases of approximately 44 and 90 kDa could phosphorylate this domain. MAP kinase and
p90rsk-dependent phosphorylation of the antiporter
could be demonstrated by immunoprecipitation of these kinases from
extracts of neonatal cardiac myocytes. PD98059, a mitogen-activated
protein kinase kinase inhibitor, decreased MAP kinase and
p90rsk phosphorylation of the antiporter and abolished serum
and endothelin 1-stimulated increases in steady-state pHi.
These results confirm the presence of MAP kinase-dependent
phosphorylation in the regulation of the Na+/H+
exchanger in the rat myocardium and suggest an important role for
p90rsk phosphorylation in regulation of the protein by
endothelin-mediated stimulation of the antiporter.
Protein Kinase-mediated Regulation of the
Na+/H+ Exchanger in the Rat Myocardium by
Mitogen-activated Protein Kinase-dependent
Pathways
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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