TY - JOUR
T1 - Diversity and regulation of amiloride-sensitive Na+ channels
AU - Benos, Dale J.
AU - Awayda, Mouhamed S.
AU - Berdiev, Bakhram K.
AU - Bradford, Anne Lynn
AU - Fuller, Catherine M.
AU - Senyk, Oksana
AU - Ismailov, Iskander I.
N1 - Funding Information:
This work was supported by NIH Grants DK37206 and HL50487.
PY - 1996
Y1 - 1996
N2 - Amiloride-sensitive Na+ channels play a vital role in many important physiological processes such as delineation of the final urine composition, sensory transduction, and whole-body Na+ homeostasis. These channels display a wide range of biophysical properties, and are regulated by cAMP-mediated second messenger systems. The first of these channels has recently been cloned. This cloned amiloride-sensitive Na+ channel is termined ENaC (Epithelial Na+ Channel) and, in heterologous cellular expression systems, displays a single channel conductance of 4 to 7 pS, a high P(Na)/P(K) (> 10), a high amiloride sensitivity (K(i)(amil) = 150 nM), and relatively long open and closed times. ENaC may form the core conduction element of many of these functionally diverse forms of Na+ channel. The kinetic and regulatory differences between these channels may be due, in large measure, to unique polypeptides that associate with the core element, forming a functional channel unit.
AB - Amiloride-sensitive Na+ channels play a vital role in many important physiological processes such as delineation of the final urine composition, sensory transduction, and whole-body Na+ homeostasis. These channels display a wide range of biophysical properties, and are regulated by cAMP-mediated second messenger systems. The first of these channels has recently been cloned. This cloned amiloride-sensitive Na+ channel is termined ENaC (Epithelial Na+ Channel) and, in heterologous cellular expression systems, displays a single channel conductance of 4 to 7 pS, a high P(Na)/P(K) (> 10), a high amiloride sensitivity (K(i)(amil) = 150 nM), and relatively long open and closed times. ENaC may form the core conduction element of many of these functionally diverse forms of Na+ channel. The kinetic and regulatory differences between these channels may be due, in large measure, to unique polypeptides that associate with the core element, forming a functional channel unit.
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U2 - 10.1038/ki.1996.237
DO - 10.1038/ki.1996.237
M3 - Article
C2 - 8743467
AN - SCOPUS:0029973443
VL - 49
SP - 1632
EP - 1637
JO - Kidney International
JF - Kidney International
SN - 0085-2538
IS - 6
ER -