Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol

Margret Oddsdottir, James R. Goldenring, Thomas E. Adrian, Michael J. Zdon, Karl A. Zucker, Irvin M. Modlin

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Histamine stimulated acid secretion is mediated by an increase in intracellular cAMP. Cytosolic protein phosphorylation stimulated by histamine was investigated in isolated rabbit parietal cells. Histamine stimulated the phosphorylation of a 30 kDa phosphoprotein with an isoelectric point of 5.6. Cimetidine completely inhibited histamine-stimulated pp30 phosphorylation. However, omeprazole had no effect on the phosphorylation of pp30. Forskolin and 8-bromo-cAMP also stimulated the phosphorylation of pp30. The results suggest that pp30 is a histamine-stimulated, cAMP-dependently phosphorylated protein substrate in parietal cell cytosol.

Original languageEnglish
Pages (from-to)489-496
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume154
Issue number2
DOIs
Publication statusPublished - Jul 29 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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