A specific histamine-stimulated phosphoprotein in isolated parietal cells.
Histamine-stimulated phosphorylation was studied in isolated rabbit parietal cells. Secretion of acid, as assessed by aminopyrine uptake, was linear at 15 min of stimulation with histamine. By utilizing two dimensional gels, a specific 30,000-Da protein (pp30) was identified whose phosphorylation was prominently stimulated by histamine after 15 min of incubation. The pp30 protein displayed an isoelectric point of 6.0. Furthermore, cAMP-dependent pp30 phosphorylation could also be demonstrated in vitro in a preparation of parietal cell cytosol. The results suggest that pp30 may represent an important histamine-stimulated cAMP-dependent phosphoprotein involved in the initiation or maintenance of parietal cell secretion.
D000632:Aminopyrine / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D000242:Cyclic AMP / Q000494:pharmacology; D005260:Female; D006632:Histamine / Q000494:pharmacology*; D007525:Isoelectric Focusing; D010295:Parietal Cells, Gastric / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits
D010710:Phosphates; D010750:Phosphoproteins; D000632:Aminopyrine; D006632:Histamine; D000242:Cyclic AMP