scholarly journals Pseudohypoaldosteronism type 1 and Liddle's syndrome mutations that affect the single-channel properties of the epithelial Na+channel

2015 ◽  
Vol 3 (11) ◽  
pp. e12600 ◽  
Author(s):  
Nina Boiko ◽  
Volodymyr Kucher ◽  
James D. Stockand
Keyword(s):  
Single Channel ◽  
Na Channel ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Channel Properties ◽  
Epithelial Na Channel ◽  
Pseudohypoaldosteronism Type

scholarly journals WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome.

1996 ◽  
Vol 15 (10) ◽  
pp. 2371-2380 ◽  
Author(s):  
O. Staub ◽  
S. Dho ◽  
P. Henry ◽  
J. Correa ◽  
T. Ishikawa ◽  
...  
Keyword(s):  
Na Channel ◽  
Ww Domains ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Epithelial Na Channel

scholarly journals Mechanism by which Liddle's syndrome mutations increase activity of a human epithelial Na+ channel

Cell ◽  
1995 ◽  
Vol 83 (6) ◽  
pp. 969-978 ◽  
Author(s):  
Peter M. Snyder ◽  
Margaret P. Price ◽  
Fiona J. McDonald ◽  
Christopher M. Adams ◽  
Kenneth A. Volk ◽  
...  
Keyword(s):  
Na Channel ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Epithelial Na Channel

scholarly journals Liddle's syndrome: A novel mouse Nedd4 isoform regulates the activity of the epithelial Na+ channel

2001 ◽  
Vol 60 (2) ◽  
pp. 466-471 ◽  
Author(s):  
Elena Kamynina ◽  
Christophe Debonneville ◽  
Robert P. Hirt ◽  
Olivier Staub
Keyword(s):  
Na Channel ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Epithelial Na Channel

scholarly journals Inhibition of the Epithelial Na+Channel by Interaction of Nedd4 with a PY Motif Deleted in Liddle’s Syndrome

1998 ◽  
Vol 273 (45) ◽  
pp. 30012-30017 ◽  
Author(s):  
Christopher C. Goulet ◽  
Kenneth A. Volk ◽  
Christopher M. Adams ◽  
Lawrence S. Prince ◽  
John B. Stokes ◽  
...  
Keyword(s):  
Na Channel ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Py Motif ◽  
Epithelial Na Channel

scholarly journals Defective regulation of the epithelial Na+ channel by Nedd4 in Liddle's syndrome

1999 ◽  
Vol 103 (5) ◽  
pp. 667-673 ◽  
Author(s):  
Hugues Abriel ◽  
Johannes Loffing ◽  
John F. Rebhun ◽  
J. Howard Pratt ◽  
Laurent Schild ◽  
...  
Keyword(s):  
Na Channel ◽  
Liddle’S Syndrome ◽  
Liddle's Syndrome ◽  
Epithelial Na Channel

The highly selective low-conductance epithelial Na channel of Xenopus laevis A6 kidney cells

1995 ◽  
Vol 269 (1) ◽  
pp. C188-C197 ◽  
Author(s):  
A. Puoti ◽  
A. May ◽  
C. M. Canessa ◽  
J. D. Horisberger ◽  
L. Schild ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Single Channel ◽  
Distal Colon ◽  
Na Channel ◽  
Kidney Cells ◽  
Rate Limiting Step ◽  
Tight Epithelia ◽  
Alpha Beta ◽  
Epithelial Na Channel

In Na-reabsorbing tight epithelia, the rate-limiting step for Na transport is the highly selective low-conductance amiloride-sensitive epithelial Na channel (type 1 ENaC). In rat distal colon, type 1 ENaC is made of three homologous subunits. The aim of this study was to identify the corresponding genes of the renal channel from the kidney-derived A6 cell line of Xenopus laevis. Three homologous subunits were identified and coexpressed in the Xenopus oocyte system. The reconstituted channel had all the characteristics of the native type 1 ENaC described in A6 cells: 1) high selectivity, 2) low single-channel conductance, 3) slow gating kinetics, and 4) high affinity for amiloride. Transcripts for alpha-, beta-, and gamma-subunits of the Xenopus epithelial Na channel (xENaC) were detected in A6 kidney cells, Xenopus kidney, lung, and to a lesser extent in stomach and skin. Each subunit of the xENaC shares approximately 60% overall identity with the corresponding rat homologue (alpha, beta, and gamma rENaC). Our data suggest that the triplication of the ENaC subunits occurred before the divergence between mammalian and amphibian lineages.

scholarly journals Regulation of the Epithelial Na+ Channel by Membrane Tension

1998 ◽  
Vol 112 (2) ◽  
pp. 97-111 ◽  
Author(s):  
Mouhamed S. Awayda ◽  
Muthangi Subramanyam
Keyword(s):  
Cytochalasin B ◽  
Single Channel ◽  
Direct Injection ◽  
Expression System ◽  
Cell Swelling ◽  
Na Channel ◽  
Bathing Solution ◽  
Membrane Tension ◽  
Whole Cell ◽  
Epithelial Na Channel

The sensitivity of αβγ rat epithelial Na+ channel (rENaC) to osmotically or mechanically induced changes of membrane tension was investigated in the Xenopus oocyte expression system, using both dual electrode voltage clamp and cell-attached patch clamp methodologies. ENaC whole-cell currents were insensitive to mechanical cell swelling caused by direct injection of 90 or 180 nl of 100-mM KCl. Similarly, ENaC whole-cell currents were insensitive to osmotic cell swelling caused by a 33% decrease of bathing solution osmolarity. The lack of an effect of cell swelling on ENaC was independent of the status of the actin cytoskeleton, as ENaC remained insensitive to osmotic and mechanical cell swelling in oocytes pretreated with cytochalasin B for 2–5 h. This apparent insensitivity of ENaC to increased cell volume and changes of membrane tension was also observed at the single channel level in membrane patches subjected to negative or positive pressures of 5 or 10 in. of water. However, and contrary to the lack of an effect of cell swelling, ENaC currents were inhibited by cell shrinking. A 45-min incubation in a 260-mosmol solution (a 25% increase of solution osmolarity) caused a decrease of ENaC currents (at −100 mV) from −3.42 ± 0.34 to −2.02 ± 0.23 μA (n = 6). This decrease of current with cell shrinking was completely blocked by pretreatment of oocytes with cytochalasin B, indicating that these changes of current are not likely related to a direct effect of cell shrinking. We conclude that αβγ rENaC is not directly mechanosensitive when expressed in a system that can produce a channel with identical properties to those found in native epithelia.

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