Phosphorylation of H,K-ATPase alpha-subunit in microsomes from rabbit gastric mucosa by cAMP-dependent protein kinase

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. Incuba...

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Veröffentlicht in:	Bioscience reports 1999-04, Vol.19 (2), p.109-114
Hauptverfasser:	Murtazina, D A, Petukhov, S P, Storey, K B, Rubtsov, A M, Lopina, O D
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cyclic AMP-Dependent Protein Kinases - metabolism Enzyme Inhibitors - pharmacology Fluorescein-5-isothiocyanate - metabolism Fluorescent Dyes - metabolism Gastric Mucosa - metabolism H(+)-K(+)-Exchanging ATPase - chemistry H(+)-K(+)-Exchanging ATPase - metabolism Microsomes - metabolism Phosphorus Radioisotopes Phosphorylation Potassium Chloride - pharmacology Proton Pump Inhibitors Rabbits Sodium Chloride - pharmacology
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Zusammenfassung:	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.
ISSN:	0144-8463 1573-4935
DOI:	10.1023/A:1020110510609