Abstract
The physiologic function of an ion pump is determined, in part, by its subcellular localization and by the cellular mechanisms that modulate its activity. The Na,K-ATPase and the gastric H,K-ATPase are two closely related members of the P-type family of ion transporting ATPases. Despite their homology, these pumps are sorted to different domains in polarized epithelial cells and their enzymatic activities are subject to distinct regulatory pathways. The molecular signals responsible for these properties have begun to be elucidated. It appears that a complex array of inter- and intra-molecular interactions govern these proteins' trafficking, distribution and catalytic capacity.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Cell Membrane / metabolism
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Cell Membrane / ultrastructure
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Cell Polarity / physiology
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Epithelial Cells / metabolism
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Epithelial Cells / ultrastructure
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Gastric Mucosa / metabolism
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H(+)-K(+)-Exchanging ATPase / chemistry
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H(+)-K(+)-Exchanging ATPase / genetics
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H(+)-K(+)-Exchanging ATPase / metabolism
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Humans
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Ion Pumps / metabolism*
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Protein Structure, Tertiary / physiology
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Protein Transport / physiology*
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Signal Transduction / physiology
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Sodium-Potassium-Exchanging ATPase / chemistry
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Sodium-Potassium-Exchanging ATPase / genetics
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Sodium-Potassium-Exchanging ATPase / metabolism
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Stomach / ultrastructure
Substances
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Ion Pumps
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Protein Isoforms
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H(+)-K(+)-Exchanging ATPase
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Sodium-Potassium-Exchanging ATPase