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


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Weinman, EJ; Steplock, D; Bui, G; Yuan, N; Shenolikar, S

Published Date

  • May 1990

Published In

Volume / Issue

  • 258 / 5 Pt 2

Start / End Page

  • F1254 - F1258

PubMed ID

  • 2159717

Pubmed Central ID

  • 2159717

International Standard Serial Number (ISSN)

  • 0002-9513

Digital Object Identifier (DOI)

  • 10.1152/ajprenal.1990.258.5.F1254


  • eng

Conference Location

  • United States