Abstract
A 100-kDa protein that is a main component of the microsomal fraction from rabbit gastric mucosa is phosphorylated by cAMP-dependent protein kinase (PKA) in the presence of 0.2% Triton X-100. Microsomes from rabbit gastric mucosa possess activity of H,K-ATPase but not activity of Na,K-ATPase. Incubation of microsomes with 5 microM fluorescein 5'-isothiocyanate (FITC) results in both an inhibition of H,K-ATPase and labeling of a protein with an electrophoretic mobility corresponding to the mobility of the protein phosphorylated by PKA. The data suggest that the alpha-subunit of H,K-ATPase can be a potential target for PKA phosphorylation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cyclic AMP-Dependent Protein Kinases / metabolism*
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Enzyme Inhibitors / pharmacology
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Fluorescein-5-isothiocyanate / metabolism
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Fluorescent Dyes / metabolism
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Gastric Mucosa / metabolism*
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H(+)-K(+)-Exchanging ATPase / chemistry
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H(+)-K(+)-Exchanging ATPase / metabolism*
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Microsomes / metabolism*
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Phosphorus Radioisotopes
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Phosphorylation
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Potassium Chloride / pharmacology
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Proton Pump Inhibitors
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Rabbits
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Sodium Chloride / pharmacology
Substances
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Enzyme Inhibitors
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Fluorescent Dyes
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Phosphorus Radioisotopes
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Proton Pump Inhibitors
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Sodium Chloride
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Potassium Chloride
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Cyclic AMP-Dependent Protein Kinases
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H(+)-K(+)-Exchanging ATPase
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Fluorescein-5-isothiocyanate