Airway function is dependent upon the regulated absorption of Na⁺ from the airway surface liquid via epithelial Na channels (ENaC), and glucocorticoid hormones are important to the control of this process. These hormones induce expression of serum and glucocorticoid inducible kinase 1 (SGK1), a kinase that phosphoryates Nedd-4/2 at Ser²²¹, Ser³²⁷, and Thr²⁴⁶, leading to the inactivation of this ubiquitin liagse. Since Nedd-4/2 normally targets ENaC for degradation, SGK1 activation is thought to increase the surface abundance of ENaC subunits leading to increased Na⁺ absorption. However, whilst we have clearly identified (perforated patch recording, n > 10) amiloride-sensitive Na⁺ currents (I_Amil) in H441 cells exposed to dexamethasone (2 mM) for 24 h, analyses of extracted protein indicated that SGK1 activity (assessed by monitoring the phosphorylation of NDRG1-Thr^346/356/366, an endogenous SGK1 substrate, n = 5) was similar to the level measured in glucocorticoid-deprived cells which do not display I_Amil. Although SGK1 activation was, however, evident after 3 h stimulation, I_Amil was negligible at this time. Subsequent experiments therefore compared (n = 3) the effects of brief (3 h) and prolonged (24 h) dexamethasone stimulation upon the phosphorylation of Nedd-4/2-Ser²²¹, -Ser³²⁷, and -Thr²⁴⁶ (antibodies obtained via C MacKintosh / P Cohen). Whilst brief exposure to dexamethasone increased the abundance of phosphorylated Nedd-4/2, there was a similar effect upon total expression. Prolonged stimulation, on the other hand, had no discernible effect upon the abundance / phosphorylation of this protein indicating that ENaC activity can be maintained independently of increased phosphorylation of Nedd-4/2.