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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5 Pt 1
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pubmed:dateCreated |
1990-1-12
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pubmed:abstractText |
In all cellular systems studied so far, the catalytic alpha- and the glycosylated beta-subunit of Na+-K+-ATPase are coordinately synthesized and are assembled into stoichiometric alpha, beta-complexes. In contrast to these data, in this study we show that the fully grown oocyte of Xenopus laevis synthesizes much less beta-subunit than alpha-subunit. The alpha-subunit produced in excess over the beta-subunit is membrane associated but highly trypsin sensitive and can be compared with the immature alpha-subunit population identified in epithelial cells immediately after synthesis (K. Geering, J. P. Kraehenbuhl, and B.C. Rossier, J. Cell Biol. 105: 2613-2619, 1987). The Xenopus oocyte thus turns out to be a unique system to study the functional role of the beta-subunit. Injection of beta-subunit-specific mRNA transcribed in vitro from a beta-cDNA clone (derived from Xenopus kidney, A6 cells) into oocytes results in translation of a glycosylated beta-subunit. The synthesis of this exogenous beta-subunit increases significantly the proportion of trypsin-resistant oocyte alpha-subunits able to perform cation-dependent conformational changes. In addition, 25-65% more ouabian binding sites are expressed at the plasma membrane in beta-mRNA-injected oocytes. In contrast, newly synthesized alpha-subunit translated after injection of size-fractionated mRNA enriched in alpha-mRNA remains trypsin sensitive as the oocyte alpha-subunit. These data suggest that association of the beta-subunit to the alpha-subunit provokes a structural rearrangement of the alpha-subunit that might be a first step toward the functional maturation of the Na+-K+-ATPase and its expression at the plasma membrane.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C851-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2556932-Animals,
pubmed-meshheading:2556932-Cell Membrane,
pubmed-meshheading:2556932-Drug Resistance,
pubmed-meshheading:2556932-Female,
pubmed-meshheading:2556932-Oocytes,
pubmed-meshheading:2556932-RNA, Messenger,
pubmed-meshheading:2556932-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:2556932-Transcription, Genetic,
pubmed-meshheading:2556932-Trypsin,
pubmed-meshheading:2556932-Xenopus
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pubmed:year |
1989
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pubmed:articleTitle |
A role for the beta-subunit in the expression of functional Na+-K+-ATPase in Xenopus oocytes.
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pubmed:affiliation |
Institut de Pharmacologie de l'Université de Lausanne, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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