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Department of Anesthesiology

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Phosphorylated Mr 32,000 dopamine- and cAMP-regulated phosphoprotein inhibits Na+,K(+)-ATPase activity in renal tubule cells.

TitlePhosphorylated Mr 32,000 dopamine- and cAMP-regulated phosphoprotein inhibits Na+,K(+)-ATPase activity in renal tubule cells.
Publication TypeJournal Article
Year of Publication1991
AuthorsAperia A, Fryckstedt J, Svensson L, Hemmings HC, Nairn AC, Greengard P
JournalProc Natl Acad Sci U S A
Volume88
Issue7
Pagination2798-801
Date Published1991 Apr 1
ISSN0027-8424
KeywordsAmino Acid Sequence, Animals, Dopamine, Dopamine and cAMP-Regulated Phosphoprotein 32, Kidney Medulla, Kidney Tubules, Kinetics, Loop of Henle, Models, Biological, Molecular Sequence Data, Molecular Weight, Nerve Tissue Proteins, Phosphopeptides, Phosphoproteins, Phosphorylation, Rats, Sodium-Potassium-Exchanging ATPase
Abstract

Dopamine inhibits Na+,K(+)-ATPase activity in several renal tubule segments and thereby regulates urinary Na+ excretion. We now show that a phosphopeptide of 31 amino acids, corresponding to residues 8-38 of the protein phosphatase inhibitor DARPP-32 (dopamine- and cAMP-regulated phosphoprotein of Mr 32,000), mimics the inhibitory action of dopamine on Na+,K(+)-ATPase activity in renal tubule cells from the ascending limb of the loop of Henle. The dephosphorylated form of the peptide is ineffective. The results indicate that dopamine acts through a protein phosphorylation pathway to regulate the activity of an ion pump. In addition, the data suggest that inhibition of protein phosphatase 1 by phophorylated DARPP-32 is a component of the mechanism by which dopamine regulates urinary Na+ excretion.

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID1849276
PubMed Central IDPMC51326
Grant ListMH 40899 / MH / NIMH NIH HHS / United States