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PMID: 1658934 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Comment

Mechanism for regulating cell surface distribution of Na+,K(+)-ATPase in polarized epithelial cells.

Science (New York, N.Y.) ·Vol. 254 ·No. 5033 ·1991-11-08 ·Pages 847-50

Hammerton RW, Krzeminski KA, Mays RW, Ryan TA, Wollner DA, Nelson WJ

Abstract

Restriction of sodium, potassium adenosine triphosphatase (Na+,K(+)-ATPase) to either the apical or basal-lateral membrane domain of polarized epithelial cells is fundamental to vectorial ion and solute transport in many tissues and organs. A restricted membrane distribution of Na+,K(+)-ATPase in Madin-Darby canine kidney (MDCK) epithelial cells was found experimentally to be generated by preferential retention of active enzyme in the basal-lateral membrane domain and selective inactivation and loss from the apical membrane domain, rather than by vectorial targeting of newly synthesized protein from the Golgi complex to the basal-lateral membrane domain. These results show how different distributions of the same subunits of Na+,K(+)-ATPase may be generated in normal polarized epithelial and in disease states.

MeSH Terms
Animals Binding Sites Cell Communication Cell Line Cell Membrane/enzymology,physiology Cell Polarity Dogs Epithelium/enzymology,physiology Kinetics Ouabain/metabolism Sodium-Potassium-Exchanging ATPase/metabolism
Chemicals
Ouabain Sodium-Potassium-Exchanging ATPase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hammerton R W
Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305-5426.
Krzeminski K A
Mays R W
Ryan T A
Wollner D A
Nelson W J
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1991-11-08
Pages
847-50
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM 35527 · United States
Corrections
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