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Phosphorylation of H,K-ATPase α-Subunit in Microsomes from Rabbit Gastric Mucosa by cAMP-Dependent Protein Kinase

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Bioscience Reports

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 μM 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 α-subunit of H,K-ATPase can be a potential target for PKA phosphorylation.

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Authors and Affiliations

  1. Department of Biochemistry, School of Biology, M.V. Lomonosov Moscow State University, Moscow, 119899, Russia

    Dilyara A. Murtazina, Alexander M. Rubtsov & Olga D. Lopina

  2. Laboratory of Enzyme Chemistry, School of Biology, M.V. Lomonosov Moscow State University, Moscow, 119899, Russia

    Sergei P. Petukhov

  3. Institute of Biochemistry, Carleton University, Ottawa, Ontario, K1S 5B6, Canada

    Kenneth B. Storey

Authors
  1. Dilyara A. Murtazina
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  2. Sergei P. Petukhov
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  3. Kenneth B. Storey
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  4. Alexander M. Rubtsov
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  5. Olga D. Lopina
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Murtazina, D.A., Petukhov, S.P., Storey, K.B. et al. Phosphorylation of H,K-ATPase α-Subunit in Microsomes from Rabbit Gastric Mucosa by cAMP-Dependent Protein Kinase. Biosci Rep 19, 109–114 (1999). https://doi.org/10.1023/A:1020110510609

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  • DOI: https://doi.org/10.1023/A:1020110510609

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