scholarly journals Hydrogen Peroxide and Sodium Transport in the Lung and Kidney

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
V. Shlyonsky ◽  
A. Boom ◽  
F. Mies

Renal and lung epithelial cells are exposed to some significant concentrations of H2O2. In urine it may reach 100 μM, while in the epithelial lining fluid in the lung it is estimated to be in micromolar to tens-micromolar range. Hydrogen peroxide has a stimulatory action on the epithelial sodium channel (ENaC) single-channel activity. It also increases stability of the channel at the membrane and slows down the transcription of the ENaC subunits. The expression and the activity of the channel may be inhibited in some other, likely higher, oxidative states of the cell. This review discusses the role and the origin of H2O2in the lung and kidney. Concentration-dependent effects of hydrogen peroxide on ENaC and the mechanisms of its action have been summarized. This review also describes outlooks for future investigations linking oxidative stress, epithelial sodium transport, and lung and kidney function.

2019 ◽  
Vol 13 (3) ◽  
pp. 036014 ◽  
Author(s):  
Mei S Yamaguchi ◽  
Mitchell M McCartney ◽  
Alexandria K Falcon ◽  
Angela L Linderholm ◽  
Susan E Ebeler ◽  
...  

1999 ◽  
Vol 277 (4) ◽  
pp. L727-L736 ◽  
Author(s):  
Naomi Niisato ◽  
Yasushi Ito ◽  
Yoshinori Marunaka

To study a cAMP-mediated signaling pathway in the regulation of amiloride-sensitive Na+ transport in rat fetal distal lung epithelial cells, we measured an amiloride-sensitive short-circuit current (Na+ transport). Forskolin, which increases the cytosolic cAMP concentration, stimulated the Na+ transport. Forskolin also activated cAMP-dependent protein kinase (PKA). A β-adrenergic agonist and cAMP mimicked the forskolin action. PKA inhibitors KT-5720, H-8, and myristoylated PKA-inhibitory peptide amide-(14—22) did not influence the forskolin action. These results suggest that forskolin stimulates Na+ transport through a PKA-independent pathway. Furthermore, forskolin increased tyrosine phosphorylation of ∼70- to 80-, ∼97-, and ∼110- to 120-kDa proteins. Protein tyrosine kinase (PTK) inhibitors (tyrphostin A23 and genistein) abolished the forskolin action. Moreover, 5-nitro-2-(3-phenylpropylamino)benzoate (a Cl−-channel blocker) prevented the stimulatory action of forskolin on Na+ transport via abolishment of the forskolin-induced cell shrinkage and tyrosine phosphorylation. Based on these results, we conclude that forskolin (and cAMP) stimulates Na+ transport in a PTK-dependent but not a PKA-dependent pathway by causing cell shrinkage, which activates PTK in rat fetal distal lung epithelial cells.


Pneumologie ◽  
2010 ◽  
Vol 64 (S 03) ◽  
Author(s):  
B Schmeck ◽  
B Dolniak ◽  
I Pollock ◽  
C Schulz ◽  
W Bertrams ◽  
...  

Pneumologie ◽  
2013 ◽  
Vol 67 (12) ◽  
Author(s):  
H Peuschel ◽  
T Ruckelshausen ◽  
C Cavelius ◽  
A Kraegeloh

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