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

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. Ci...

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Veröffentlicht in:	Biochemical and biophysical research communications 1988-07, Vol.154 (2), p.489-496
Hauptverfasser:	Oddsdottir, Margret, Goldenring, James R., Adrian, Thomas E., Zdon, Michael J., Zucker, Karl A., Modlin, Irvin M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cimetidine - pharmacology Cyclic AMP - pharmacology Cytosol - analysis Fundamental and applied biological sciences. Psychology Histamine - pharmacology Isoelectric Point Miscellaneous Molecular Weight Parietal Cells, Gastric - analysis Parietal Cells, Gastric - drug effects Phosphoproteins - analysis Phosphorylation Proteins Rabbits
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Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(88)90166-0