Direct Activation of Gastric H,K-ATPase by N-Terminal Protein Kinase C Phosphorylation. Comparison of the Acute Regulation Mechanisms of H,K-ATPase and Na,K-ATPase

In this study we compared the protein kinase dependent regulation of gastric H,K-ATPase and Na,K-ATPase. The protein kinase A/protein kinase C (PKA/PKC) phosphorylation profile of H,K-ATPase was very similar to the one found in the Na,K-ATPase. PKC phosphorylation was taking place in the N-terminal...

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Veröffentlicht in:	Biophysical journal 2003-03, Vol.84 (3), p.1690-1700
Hauptverfasser:	Cornelius, Flemming, Mahmmoud, Yasser A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Catalysis Cells, Cultured Channels, Receptors, and Transporters Enzyme Activation Gastric Mucosa - enzymology Gastric Mucosa - metabolism H(+)-K(+)-Exchanging ATPase - chemistry H(+)-K(+)-Exchanging ATPase - metabolism Homeostasis - physiology Molecular biology Molecular Sequence Data Multienzyme Complexes - metabolism Parietal Cells, Gastric - enzymology Parietal Cells, Gastric - metabolism Phosphorylation Protein Kinase C - chemistry Protein Kinase C - metabolism Protein Subunits Proteins Sodium-Potassium-Exchanging ATPase - chemistry Sodium-Potassium-Exchanging ATPase - metabolism Swine
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