Comparison of the Osmolyte Transport Properties Induced by trAE1 versus IClswell in Xenopus Oocytes

Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase. In addition to this shared function, FXYD3 displays some uncommon characteristics. First, in contrast to other FXYD proteins, which were shown to be type I membrane proteins, FXYD3 may have a second transmembrane-like domain because of the presence of a noncleavable signal peptide. Second, FXYD3 can associate with Na,K- as well as H,K-ATPases when expressed in Xenopus oocytes. However, in situ (stomach), FXYD3 is associated only with Na,K-ATPase because its expression is restricted to mucous cells in which H,K-ATPase is absent. Coexpressed in Xenopus oocytes, FXYD3 modulates the glycosylation processing of the β subunit of X,K-ATPase dependent on the presence of the signal peptide. Finally, FXYD3 decreases both the apparent affinity for Na+ and K+ of Na,K-ATPase.

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Revisiting the functional properties of NPF6.3/NRT1.1/CHL1 in xenopus oocytes

10.1101/244467 ◽

2018 ◽

Cited By ~ 2

Author(s):

Mélanie Noguero ◽

Sophie Léran ◽

Eléonore Bouguyon ◽

Chantal Brachet ◽

Pascal Tillard ◽

...

Keyword(s):

Transport Properties ◽

Xenopus Oocytes ◽

Nitrate Concentration ◽

Functional Characterization ◽

Nitrate Transport ◽

Experimental Conditions ◽

Point Mutant ◽

Electrode Voltage ◽

Nitrate Transporters

ABSTRACTWithin the Arabidopsis NPF proteins, most of the characterized nitrate transporters are low-affinity transporters, whereas the functional characterization of NPF6.3/NRT1.1 has revealed interesting transport properties: the transport of nitrate and auxin, the eletrogenicity of the nitrate transport and a dual-affinity transport behavior for nitrate depending on external nitrate concentration. However, some of these properties remained controversial and were challenged here. We functionally express WT NPF6.3/NRT1.1 and some of its mutant in Xenopus oocytes and used a combination of uptake experiments using 15N-labelled nitrate and two-electrode voltage-clamp. In our experimental conditions in xenopus oocytes, in the presence or in the absence of external chloride, NPF6.3/NRT1.1 behaves as a non-electrogenic and pure low-affinity transporter. Moreover, further functional characterization of a NPF6.3/NRT1.1 point mutant, P492L, allowed us to hypothesize that NPF6.3/NRT1.1 is regulated by internal nitrate concentration and that the internal perception site involves the P492 residue.

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Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different β-subunits

AJP Cell Physiology ◽

10.1152/ajpcell.00590.2001 ◽

2002 ◽

Vol 283 (1) ◽

pp. C305-C314 ◽

Cited By ~ 32

Author(s):

Gilles Crambert ◽

Jean-Daniel Horisberger ◽

Nikolai N. Modyanov ◽

Käthi Geering

Keyword(s):

Cell Surface ◽

Transport Properties ◽

Functional Properties ◽

Conformational Changes ◽

Xenopus Oocytes ◽

Structural Integrity ◽

Catalytic Subunit ◽

Α Subunit ◽

Distinct Effect ◽

New Evidence

To investigate whether nongastric H+-K+-ATPases transport Na+ in exchange for K+ and whether different β-isoforms influence their transport properties, we compared the functional properties of the catalytic subunit of human nongastric H+-K+-ATPase, ATP1al1 (AL1), and of the Na+-K+-ATPase α1-subunit (α1) expressed in Xenopus oocytes, with different β-subunits. Our results show that βHK and β1-NK can produce functional AL1/β complexes at the oocyte cell surface that, in contrast to α1/β1 NK and α1/βHK complexes, exhibit a similar apparent K+ affinity. Similar to Na+-K+-ATPase, AL1/β complexes are able to decrease intracellular Na+ concentrations in Na+-loaded oocytes, and their K+ transport depends on intra- and extracellular Na+ concentrations. Finally, controlled trypsinolysis reveals that β-isoforms influence the protease sensitivity of AL1 and α1 and that AL1/β complexes, similar to the Na+-K+-ATPase, can undergo distinct K+-Na+- and ouabain-dependent conformational changes. These results provide new evidence that the human nongastric H+-K+-ATPase interacts with and transports Na+ in exchange for K+ and that β-isoforms have a distinct effect on the overall structural integrity of AL1 but influence its transport properties less than those of the Na+-K+-ATPase α-subunit.

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Spectroscopic Diagnostics of Tokamaks

International Astronomical Union Colloquium ◽

10.1017/s0252921100107638 ◽

1988 ◽

Vol 102 ◽

pp. 165-174

Author(s):

C. de Michelis

Keyword(s):

Transport Properties ◽

Power Losses ◽

Spectroscopic Diagnostics ◽

Important Concern

AbstractImpurities being an important concern in tokamaks, spectroscopy plays a key role in their understanding. Techniques for the evaluation of concentrations, power losses and transport properties are surveyed, and a few developments are outlined.

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Structure and Orientation of As Precipitates in LT-MBE Grown GaAs

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100088816 ◽

1991 ◽

Vol 49 ◽

pp. 900-901 ◽

Cited By ~ 1

Author(s):

Alain Claverie ◽

Zuzanna Liliental-Weber

Keyword(s):

Transport Properties ◽

Layer Thickness ◽

Growth Temperature ◽

Low Temperatures ◽

Lattice Parameter ◽

Crystalline Quality ◽

Insulating Properties ◽

Lt Gaas

GaAs layers grown by MBE at low temperatures (in the 200°C range, LT-GaAs) have been reported to have very interesting electronic and transport properties. Previous studies have shown that, before annealing, the crystalline quality of the layers is related to the growth temperature. Lowering the temperature or increasing the layer thickness generally results in some columnar polycrystalline growth. For the best “temperature-thickness” combinations, the layers may be very As rich (up to 1.25%) resulting in an up to 0.15% increase of the lattice parameter, consistent with the excess As. Only after annealing are the technologically important semi-insulating properties of these layers observed. When annealed in As atmosphere at about 600°C a decrease of the lattice parameter to the substrate value is observed. TEM studies show formation of precipitates which are supposed to be As related since the average As concentration remains almost unchanged upon annealing.

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