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

作者信息

Oddsdottir M, Goldenring J R, Adrian T E, Zdon M J, Zucker K A, Modlin I M

机构信息

Department of Surgery, Yale University School of Medicine, West Haven, Connecticut.

出版信息

Biochem Biophys Res Commun. 1988 Jul 29;154(2):489-96. doi: 10.1016/0006-291x(88)90166-0.

DOI:10.1016/0006-291x(88)90166-0
PMID:2840899
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.

摘要

相似文献

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Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol.
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Small GTP-binding proteins in parietal cells: candidate modulators of parietal cell membrane dynamics.壁细胞中的小GTP结合蛋白:壁细胞膜动力学的候选调节因子。
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Yale J Biol Med. 1992 Nov-Dec;65(6):561-76; discussion 621-3.