1. Bioinformatic Study of Possible Acute Regulation of Acid Secretion in the Stomach.
- Author
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Lee, Yan Hay Grace, Cerf, Nicole T., Shalaby, Nicholas, Montes, Mónica R., and Clarke, Ronald J.
- Subjects
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PARIETAL cells , *PROTEIN kinase C , *GASTRIC acid , *PROTEIN kinases , *AMINO acid sequence , *MEMBRANE proteins , *GASTRIC mucosa - Abstract
The gastric H+,K+-ATPase is an integral membrane protein which derives energy from the hydrolysis of ATP to transport H+ ions from the parietal cells of the gastric mucosa into the stomach in exchange for K+ ions. It is responsible for the acidic environment of the stomach, which is essential for digestion. Acid secretion is regulated by the recruitment of the H+,K+-ATPase from intracellular stores into the plasma membrane on the ingestion of food. The similar amino acid sequences of the lysine-rich N-termini α-subunits of the H+,K+- and Na+,K+-ATPases, suggests similar acute regulation mechanisms, specifically, an electrostatic switch mechanism involving an interaction of the N-terminal tail with the surface of the surrounding membrane and a modulation of the interaction via regulatory phosphorylation by protein kinases. From a consideration of sequence alignment of the H+,K+-ATPase and an analysis of its coevolution with protein kinase C and kinases of the Src family, the evidence points towards a phosphorylation of tyrosine-7 of the N-terminus by either Lck or Yes in all vertebrates except cartilaginous fish. The results obtained will guide and focus future experimental research. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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