The anion specificity of the sodium-potassium-chloride cotransporter in rabbit kidney outer medulla: studies on medullary plasma membranes

1986 ◽  
Vol 407 (S2) ◽  
pp. S168-S173 ◽  
Author(s):  
R. Kinne ◽  
E. Kinne-Saffran ◽  
B. Sch�lermann ◽  
H. Sch�tz
Keyword(s):  
Potassium Chloride ◽  
Plasma Membranes ◽  
Rabbit Kidney ◽  
Outer Medulla ◽  
Sodium Potassium ◽  
Sodium Potassium Chloride Cotransporter

PGE2MEDIATES OENOCYTOID CELL LYSIS VIA A SODIUM-POTASSIUM-CHLORIDE COTRANSPORTER

2015 ◽  
Vol 89 (4) ◽  
pp. 218-229 ◽  
Author(s):  
Sony Shrestha ◽  
Jiyeong Park ◽  
Seung-Joon Ahn ◽  
Yonggyun Kim
Keyword(s):  
Potassium Chloride ◽  
Cell Lysis ◽  
Sodium Potassium ◽  
Sodium Potassium Chloride Cotransporter

scholarly journals Ultrastructural localization of Na+,K+-ATPase in rat and rabbit kidney medulla.

1981 ◽  
Vol 91 (3) ◽  
pp. 803-813 ◽  
Author(s):  
S A Ernst ◽  
J H Schreiber
Keyword(s):  
Plasma Membranes ◽  
Rat Kidney ◽  
Ultrastructural Localization ◽  
Urine Concentration ◽  
Rabbit Kidney ◽  
Significant Activity ◽  
Outer Medulla ◽  
Kidney Medulla ◽  
Cytochemical Localization ◽  
Collecting Tubules

Na+,K+-ATPase was localized at the ultrastructural level in rat and rabbit kidney medulla. The cytochemical method for the K+-dependent phosphatase component of the enzyme, using p-nitrophenylphosphate (NPP) as substrate, was employed to demonstrate the distribution of Na+, K+-ATPase in tissue-chopped sections from kidneys perfusion-fixed with 1% paraformaldehyde-0.25% glutaraldehyde. In other outer medulla of rat kidney, ascending thick limbs (MATL) were sites of intense K+-dependent NPPase (K+-NPPase) activity, whereas descending thick limbs and collecting tubules were barely reactive. Although descending thin limbs (DTL) of short loop nephrons were unstained, DTL from long loop nephrons in outer medulla were sites of moderate K+-NPPase activity. In rat inner medulla, DTL and ascending thin limbs (ATL) were unreactive for K+-NPPase. In rabbit medulla, only MATL were sites of significant K+-NPPase activity. The specificity of the cytochemical localization of Na+,K+-ATPase at reactive sites in rat and rabbit kidney medulla was demonstrated by K+-dependence of reaction product deposition, localization of reaction product (precipitated phosphate hydrolyzed from NPP) to the cytoplasmic side of basolateral plasma membranes, insensitivity of the reaction to inhibitors of nonspecific alkaline phosphatase, and, in the glycoside-sensitive rabbit kidney, substantial inhibition of staining by ouabain. The observed pattern of distribution of the sodium transport enzyme in kidney medulla is particularly relevant to current models for urine concentration. The presence of substantial Na+,K+-ATPase in MATL is consistent with the putative role of this segment as the driving force for the countercurrent multiplication system in the outer medulla. The absence of significant activity in inner medullary ATL and DTL, however, implies that interstitial solute accumulation in this region probably occurs by passive processes. The localization of significant Na+,K+-ATPase in outer medullary DTL of long loop nephrons in the rat suggests that solute addition in this segment may occur in part by an active salt secretory mechanism that could ultimately contribute to the generation of inner medullary interstitial hypertonicity and urine concentration.

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