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  Phosphorylation of the alpha-subunits of the Na+/K+-ATPase from mammalian kidneys and Xenopus oocytes by cGMP-dependent protein kinase results in stimulation of ATPase activity

Fotis, H., Tatjanenko, L. V., & Vasilets, L. A. (1999). Phosphorylation of the alpha-subunits of the Na+/K+-ATPase from mammalian kidneys and Xenopus oocytes by cGMP-dependent protein kinase results in stimulation of ATPase activity. European Journal of Biochemistry, 260(3), 904-910. doi:10.1046/j.1432-1327.1999.00237.x.

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 Creators:
Fotis, Heike1, Author              
Tatjanenko, Liliya V. 2, Author
Vasilets, Larisa A.1, 2, Author              
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Institute of Chemical Physics Research, Russian Academy of Sciences, Chernogolovka, Russia, ou_persistent22              

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Free keywords: cGMP; kidney; Na+; K+‐ATPase; phosphorylation; PKG
 Abstract: Phosphorylation of Na+/K+‐ATPase by cGMP‐dependent protein kinase (PKG) has been studied in enzymes purified from pig, dog, sheep and rat kidneys, and in Xenopus oocytes. PKG phosphorylates the α‐subunits of all animal species investigated. Phosphorylation of the β‐subunit was not observed. The stoichiometry of phosphorylation estimated for pig, sheep and dog renal Na+/K+‐ATPase is 3.5, 2.2 and 2.1 mol Pi per mol α‐subunit, respectively. Proteolytic fingerprinting of the pig α1‐subunits phosphorylated by PKG using specific antibodies raised against N‐terminus or C‐terminus reveals that phosphorylation sites are located within the intracellular loop of the α‐subunit between the 35 kDa N‐terminal and 27 kDa C‐terminal fragments. Phosphorylation sites within the α1‐subunit of the purified Na+/K+‐ATPase do not appear to be easily accessible for PKG since incorporation of Pi requires 0.2% of Triton X‐100. Administration of cGMP and PKG in the presence of 5 mm ATP, which prevents inactivation of the Na+/K+‐ATPase by detergent, leads to stimulation of hydrolytic activity by 61%. Administration of 50 µm of cGMP or dbcGMP in yolk‐free homogenates of Xenopus oocytes leads to stimulation of ouabain‐dependent ATPase activity by 130–198% and to incorporation of 33P into the α‐subunit without the detergent. Hence, PKG plays regulatory role in active transmembraneous transport of Na+ and K+ via phosphorylation of the catalytic subunit of the Na+/K+‐ATPase.

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Language(s): eng - English
 Dates: 1998-12-221998-10-221999-01-132001-12-251999-03-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1046/j.1432-1327.1999.00237.x
PMID: 10103022
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 260 (3) Sequence Number: - Start / End Page: 904 - 910 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040