Am J Physiol Cell Physiol Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 276: C109-C119, 1999;
0363-6143/99 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Marshall, L. J.
Right arrow Articles by Mehta, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Marshall, L. J.
Right arrow Articles by Mehta, A.
Vol. 276, Issue 1, C109-C119, January 1999

Na+ and K+ regulate the phosphorylation state of nucleoside diphosphate kinase in human airway epithelium

L. J. Marshall, R. Muimo, C. E. Riemen, and A. Mehta

Department of Child Health, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, United Kingdom

We describe how cations, in the presence of ATP, regulate the phosphorylated form of 19- and 21-kDa nucleoside diphosphate kinase (NDPK; EC 2.7.4.6), a kinase controlling K+ channels, G proteins, cell secretion, cellular energy production, and UTP synthesis. In apically enriched human nasal epithelial membranes, 10 mM Na+ inhibits phosphorylation of NDPK relative to other cations. Dose response showed that, whereas K+ induces a fourfold greater phosphate incorporation (EC50 10 mM), Na+ is inhibitory (EC50 10 mM) compared with respective buffer controls. Cation discrimination is nucleotide selective (not seen with [gamma -32P]GTP) and NDPK specific (not seen with p37h, a previously characterized Cl--sensitive phosphoprotein). Na+ does not exert an inhibitory effect on NDPK phosphorylation directly but is likely to act via an okadaic acid-insensitive phosphatase. We speculate that the ability of NDPK to discriminate between physiologically relevant cation concentrations provides a novel example of cross talk within the apical membrane.

membrane; phosphatase; nucleotide; adenosine 5'-triphosphate; chloride


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
I. Rishal, T. Keren-Raifman, D. Yakubovich, T. Ivanina, C. W. Dessauer, V. Z. Slepak, and N. Dascal
Na+ Promotes the Dissociation between Galpha GDP and Gbeta gamma , Activating G Protein-gated K+ Channels
J. Biol. Chem., January 31, 2003; 278(6): 3840 - 3845.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Muimo, Z. Hornickova, C. E. Riemen, V. Gerke, H. Matthews, and A. Mehta
Histidine Phosphorylation of Annexin I in Airway Epithelia
J. Biol. Chem., November 17, 2000; 275(47): 36632 - 36636.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online