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Epithelial sodium channel regulated by aldosterone-induced protein sgk.
- S. Y. Chen, A. Bhargava, D. Pearce
- Biology, MedicineProceedings of the National Academy of Sciences…
- 2 March 1999
Sgk (serum and glucocorticoid-regulated kinase), a member of the serine-threonine kinase family, is identified as an aldosterone-induced regulator of ENaC activity, suggesting that sgk plays a central role in ald testosterone regulation of Na+ absorption and thus in the control of extracellular fluid volume, blood pressure, and sodium homeostasis.
Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family
The permease-related protein E16 is identified as the first light chain of h4F2hc and it is shown that the resulting heterodimeric complex mediates L-type amino-acid transport.
Characterization of early aldosterone-induced RNAs identified in A6 kidney epithelia
The characteristics of RNA accumulation and their time courses suggest a possible role of one of these induced RNAs in the mediation of the early effect of aldosterone on Na transport.
Ras pathway activates epithelial Na+ channel and decreases its surface expression in Xenopus oocytes.
The possibility that XK-Ras2A, which is the first regulatory protein known to be transcriptionally induced by aldosterone, could play a role in the control of XENaC function in a Aldosterone target cells is raised.
Pleiotropic action of aldosterone in epithelia mediated by transcription and post-transcription mechanisms.
The aldosterone-induced increase in sodium reabsorption across tight epithelia can be divided schematically into two functional phases: an early regulatory phase starting after a lag period of 20 to…
Role of SGK in mineralocorticoid-regulated sodium transport.
The data suggest that SGK is an important mediator of aldosterone effects on Na+ transport in tight epithelia and is an ancient kinase that was adapted to the control of epithelialNa+ transport by early vertebrates as they made the transition from a marine to a freshwater environment.
Adenosine inhibits the transfected Na+‐H+ exchanger NHE3 in Xenopus laevis renal epithelial cells (A6/C1)
CPA inhibits rat NHE3 expressed apically in A6 epithelia via both the apical PKC‐coupled A1 and the basolateral PKA‐cOUpled A2 adenosine receptors.
cAMP sensitivity conferred to the epithelial Na+ channel by α-subunit cloned from guinea-pig colon
- M. Schnizler, L. Mastroberardino, F. Reifarth, W. Weber, F. Verrey, W. Clauss
- BiologyPflügers Archiv
- 18 February 2000
It is shown here that membrane-permeant cAMP can activate ENaC expressed in Xenopus oocytes (3.8-fold) upon replacement of the rat α-subunit by a new α- subunit cloned from guinea-pig colon (gpα), which raises the possibility that cAMP could stimulate ENaCs by different mechanisms.
Aldosterone modulates sodium kinetics of Na,K-ATPase containing an alpha 1 subunit in A6 kidney cell epithelia.
- J. Beron, L. Mastroberardino, A. Spillmann, F. Verrey
- Biology, MedicineMolecular biology of the cell
- 1 March 1995
In conclusion, aldosterone acts on Na pumps containing an alpha 1 subunit in two ways: during its early phase of action it stimulates their transport activity by increasing their apparent Na affinity at physiological intracellular Na concentrations, and in the long term it produces an increase in the maximal transport capacity, which corresponds to the known increase to the number of Na pumps.