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Regulation of renal Na(+)-H+ exchanger by cAMP-dependent protein kinase.

Publication ,  Journal Article
Weinman, EJ; Steplock, D; Bui, G; Yuan, N; Shenolikar, S
Published in: Am J Physiol
May 1990

Octyl glucoside-extracted rabbit renal brush-border membrane (BBM) proteins were sequentially fractionated using anion exchange chromatography, and the fractions were tested for Na(+)-H+ exchange activity, amiloride sensitivity, and the effect of adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) after reconstitution into artificial lipid vesicles. Compared with the initial protein extract, an anionic protein fraction eluting with 0.2-0.4 M NaCl (fraction B) demonstrated increased Na(+)-H+ exchange activity. Fraction B also demonstrated sensitivity to inhibition by amiloride but was not regulated by PKA. Co-reconstitution of fraction B with a BBM protein fraction highly enriched in a 42-kDa polypeptide restored the inhibitory response to PKA. These experiments suggest that, as assayed in a solubilized and reconstituted system, the Na(+)-H+ exchanger contains a dissociable PKA regulatory component, possibly a polypeptide of 42 kDa.

Duke Scholars

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

May 1990

Volume

258

Issue

5 Pt 2

Start / End Page

F1254 / F1258

Location

United States

Related Subject Headings

  • Sodium-Hydrogen Exchangers
  • Sodium
  • Proteins
  • Protein Kinases
  • Phosphorylation
  • Microvilli
  • Liposomes
  • Kidney
  • Hydrogen-Ion Concentration
  • Electrophoresis, Polyacrylamide Gel
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Weinman, E. J., Steplock, D., Bui, G., Yuan, N., & Shenolikar, S. (1990). Regulation of renal Na(+)-H+ exchanger by cAMP-dependent protein kinase. Am J Physiol, 258(5 Pt 2), F1254–F1258. https://doi.org/10.1152/ajprenal.1990.258.5.F1254

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

May 1990

Volume

258

Issue

5 Pt 2

Start / End Page

F1254 / F1258

Location

United States

Related Subject Headings

  • Sodium-Hydrogen Exchangers
  • Sodium
  • Proteins
  • Protein Kinases
  • Phosphorylation
  • Microvilli
  • Liposomes
  • Kidney
  • Hydrogen-Ion Concentration
  • Electrophoresis, Polyacrylamide Gel