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. 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.
Oddsdottir
M
M
Department of Surgery, Yale University School of Medicine, West Haven, Connecticut.
Goldenring
J R
JR
Adrian
T E
TE
Zdon
M J
MJ
Zucker
K A
KA
Modlin
I M
IM
D000818:Animals; D002927:Cimetidine / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology; D003600:Cytosol / Q000032:analysis; D006632:Histamine / Q000494:pharmacology*; D007526:Isoelectric Point; D008970:Molecular Weight; D010295:Parietal Cells, Gastric / Q000032:analysis* / Q000187:drug effects; D010750:Phosphoproteins / Q000032:analysis*; D010766:Phosphorylation; D011817:Rabbits
D010750:Phosphoproteins; D002927:Cimetidine; D006632:Histamine; D000242:Cyclic AMP