Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits
- C. Canessa, L. Schild, B. Rossier
- BiologyNature
- 3 February 1994
The ion-selective permeability, the gating properties and the pharmacological profile of the channel formed by coexpressing the three subunits in oocytes are similar to that of the native channel.
Distribution of transcellular calcium and sodium transport pathways along mouse distal nephron.
- J. Loffing, D. Loffing‐Cueni, B. Kaissling
- BiologyAJP - Renal Physiology
- 1 December 2001
DCT2 and CNT are disclosed as major sites for transcellular Ca(2+) transport in the mouse distal nephron, which suggests their mutual interactions in transport regulation.
Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1
- Sue S. Chang, S. Grunder, R. Lifton
- Biology, MedicineNature Genetics
- 1 March 1996
Investigation of affected offspring of consanguineous union reveals mutations in either the α or β subunits of the amiloride-sensitive epithelial sodium channel in five kindreds that demonstrate the molecular basis and explain the pathophysiology of this disease.
An epithelial serine protease activates the amiloride-sensitive sodium channel
- V. Vallet, A. Chraibi, H. Gaeggeler, J. Horisberger, B. Rossier
- BiologyNature
- 9 October 1997
This work cloned a 329-residue protein belonging to the serine protease family and shows that coexpression of this protein with ENaC in Xenopus oocytes increases the activity of the sodiumchannel by two- to threefold.
Epithelial sodium channel related to proteins involved in neurodegeneration
- C. Canessa, J. Horisberger, B. Rossier
- BiologyNature
- 4 February 1993
The gene encoding this rat sodium channel subunit shares significant sequence similarity with mec-4 and deg-1, members of a family of Caenorhabditis elegans genes involved in sensory touch transduction and, when mutated, neuronal degeneration, and it is proposed that the gene products of these three genes are member of a gene family coding for cation channels.
Lithium nephrotoxicity revisited
- J. Grünfeld, B. Rossier
- Medicine, BiologyNature Reviews Nephrology
- 1 May 2009
Clinical and clinical evidence demonstrates the efficacy of the ENaC inhibitor amiloride for the treatment of lithium-induced NDI; however, whether this agent can prevent the long-term adverse effects of lithium is not yet known.
Corticosteroid-dependent sodium transport in a novel immortalized mouse collecting duct principal cell line.
- M. Bens, V. Vallet, A. Vandewalle
- BiologyJournal of the American Society of Nephrology
- 1 May 1999
This new immortalized mammalian CCD clonal cell line has retained a high level of epithelial differentiation and sodium transport stimulated by aldosterone and therefore represents a useful mammalian cell system for identifying the genes controlled by a Aldosterone.
Aldosterone induces rapid apical translocation of ENaC in early portion of renal collecting system: possible role of SGK.
- J. Loffing, M. Zečević, F. Verrey
- Biology, MedicineAJP - Renal Physiology
- 1 April 2001
It is shown by real-time RT-PCR and immunofluorescence that an aldosterone injection in adrenalectomized rats induces alpha-ENaC subunit expression along the entire ASDN within 2 h, whereas beta- and gamma- ENaC are constitutively expressed.
Mineralocorticoid versus glucocorticoid receptor occupancy mediating aldosterone-stimulated sodium transport in a novel renal cell line.
- H. Gaeggeler, E. Gonzalez-Rodriguez, B. Rossier
- BiologyJournal of the American Society of Nephrology
- 1 April 2005
Within the physiologic range of aldosterone concentrations, sodium transport is predicted to be controlled by MR occupancy during circadian cycles and by MR and GR occupancy during salt restriction or acute stress.
Membrane topology of the epithelial sodium channel in intact cells.
- C. Canessa, A. Mérillat, B. Rossier
- BiologyAmerican Journal of Physiology
- 1 December 1994
The highly selective amiloride-sensitive epithelial sodium channel is formed of three homologous subunits termed alpha-, beta-, and gamma-rENaC, and all three subunits are glycosylated in a cell-free translation assay, demonstrating that they share in vitro a common pattern of membrane insertion.
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