Amiloride directly inhibits the Na,K-ATPase activity of rabbit kidney proximal tubules

Science ◽  
1983 ◽  
Vol 220 (4600) ◽  
pp. 957-958 ◽  
Author(s):  
S. Soltoff ◽  
L. Mandel
Keyword(s):  
Atpase Activity ◽  
Proximal Tubules ◽  
Rabbit Kidney ◽  
Kidney Proximal Tubules

Ouabain-insensitive, Na-ATPase activity in pure suspensions of rat kidney proximal tubules

FEBS Letters ◽  
1990 ◽  
Vol 269 (1) ◽  
pp. 77-78 ◽  
Author(s):  
Reinaldo Marín ◽  
Daniela C. Gómez ◽  
Gloria A. Rodríguez ◽  
Teresa Proverbio ◽  
Fulgencio Proverbio
Keyword(s):  
Atpase Activity ◽  
Rat Kidney ◽  
Proximal Tubules ◽  
Kidney Proximal Tubules

Localization of NaPi-1, a Na-Pi cotransporter, in rabbit kidney proximal tubules

1993 ◽  
Vol 424 (3-4) ◽  
pp. 203-209 ◽  
Author(s):  
Maria Custer ◽  
Felix Meier ◽  
Eberhard Schlatter ◽  
Rainer Greger ◽  
Arlyn Garcia-Perez ◽  
...  
Keyword(s):  
Proximal Tubules ◽  
Rabbit Kidney ◽  
Kidney Proximal Tubules

Localization of NaPi-1, a Na/Pi cotransporter, in rabbit kidney proximal tubules

1993 ◽  
Vol 424 (3-4) ◽  
pp. 210-215 ◽  
Author(s):  
J. Biber ◽  
M. Custer ◽  
A. Werner ◽  
B. Kaissling ◽  
H. Murer
Keyword(s):  
Proximal Tubules ◽  
Rabbit Kidney ◽  
Kidney Proximal Tubules

scholarly journals Transport ATPase cytochemistry: ultrastructural localization of potassium-dependent and potassium-independent phosphatase activities in rat kidney cortex.

1975 ◽  
Vol 66 (3) ◽  
pp. 586-608 ◽  
Author(s):  
S A Ernst
Keyword(s):  
Alkaline Phosphatase ◽  
Atpase Activity ◽  
Rat Kidney ◽  
Proximal Tubules ◽  
Rabbit Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Distal Tubules ◽  
Extracellular Side ◽  
Collecting Tubules

A cytochemical method for the light and electron microscope localization of the K- and Mg-dependent phosphatase component of the Na-K-ATPase complex was applied to rat kidney cortex, utilizing p-nitrophenylphosphate (NPP) as substrate. Localization of K-N-ATPase activity in kidneys fixed by perfusion with 1% paraformaldehyde -0.25% glutaraldehyde demonstrated that distal tubules are the major cortical site for this sodium transport enzyme. Cortical collecting tubules were moderately reactive, whereas activity in proximal tubules was resolved only after short fixation times and long incubations. In all cases, K-NPPase activity was restricted to the cytoplasmic side of the basolateral plasma membranes, which are characterized in these neplron segments by elaborate folding of the cell surface. Although the rat K-NPPase appeared almost completely insensitive to ouabain with this cytochemical medium, parallel studies with the more glycoside-sensitive rabbit kidney indicated that K-NPPase activity in these nephron segments is sensitive to this inhibitor. In addition to K-NPPase, nonspecific alkaline phosphatase also hydrolyzed NPP. The latter could be differentiated cytochemically from the specific phosphatase, since alkaline phosphatase was K-independent, insensitive to ouabain, and specifically inhibited by cysteine. Unlike K-NPPPase, alkaline phosphatase was localized primarily to the extracellular side of the microvillar border of proximal tubules. A small amount of cysteine-sensitive activity was resolved along peritubular surfaces of proximal tubules. Distal tubules were unreactive. In comparative studies, Mg-ATPase activity was localized along the extracellular side of the luminal and basolateral surfaces of proximal and distal tubules and the basolateral membranes of collecting tubules.

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