Proton pump activity and Mg-ATPase activity in rat kidney cortex brushborder membranes: effect of ?proton ATPase? inhibitors

1986 ◽  
Vol 407 (S2) ◽  
pp. S180-S185 ◽  
Author(s):  
E. Kinne-Saffran ◽  
R. Kinne
Keyword(s):  
Atpase Activity ◽  
Proton Pump ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Proton Atpase ◽  
Atpase Inhibitors ◽  
Pump Activity

Time course of the renal response to triiodothyronine in the rat

1979 ◽  
Vol 236 (1) ◽  
pp. F9-F13
Author(s):  
C. S. Lo ◽  
T. N. Lo
Keyword(s):  
Glomerular Filtration Rate ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Filtration Rate ◽  
Time Course ◽  
Rat Kidney ◽  
Secondary Response ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Early Increase

Experiments were carried out to compare temporal changes in glomerular filtration rate (GFR), filtered Na+ load, and renal cortical (Na+ + K+)-adenosine triphosphatase (Na-K-ATPase) activity in the hypothyroid rat after administration of a single dose of triiodothyronine (T3) (50 microgram/100 g body wt). The cortex showed an increase in Na-K-ATPase at 24 h and progressive increases to a peak of 62% at 48 h. GFR and filtered Na+ load showed no changes at 24 and 48 h. At 72h, however, significant increases of 62 and 63% (per rat) were observed in GFR and filtered Na+ load, respectively. The results show that the early increase in Na-K-ATPase activity upon T3 treatment precedes the increases in GFR and filtered Na+ load, suggesting a direct effect of T3 on the regulation of Na-K-ATPase activity in the hypothyroid rat kidney cortex, rather than a secondary response to a primary increase in filtered Na+ load as proposed previously.

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.

Reconstitution and partial purification of calcium transport activity from rat kidney cortex

1992 ◽  
Vol 263 (2) ◽  
pp. F192-F200 ◽  
Author(s):  
K. Sugimura ◽  
J. Abramowitz ◽  
Y. Tsukamoto ◽  
W. N. Suki
Keyword(s):  
Atpase Activity ◽  
Rat Kidney ◽  
Gradient Centrifugation ◽  
Basolateral Membrane ◽  
High Capacity ◽  
Partial Purification ◽  
Kidney Cortex ◽  
Uptake System ◽  
Rat Kidney Cortex ◽  
Uptake Activity

An ATP-dependent Ca2+ uptake system from rat renal cortical basolateral membranes was solubilized with Triton X-100 and reconstituted into liposomes with lecithin. In the presence of Mg2+, Ca2+ uptake in the reconstituted vesicles was time and ATP dependent and was inhibited by vanadate. Ca2+ uptake in basolateral membrane vesicles depleted of endogenous calmodulin was enhanced by exogenous calmodulin and depressed by R-24571. This sensitivity to calmodulin and R-24571 was lost upon reconstitution in the presence and absence of leupeptin. Vesicles containing Ca2+ uptake activity were separated by gradient centrifugation after Ca2+ was taken up and accumulated as calcium phosphate in the vesicles. This resulted in Ca2+ uptake activity that was enriched 25 times. However, Ca(2+)-dependent adenosinetriphosphatase (ATPase) activity was not enriched significantly. This Ca(2+)-ATPase had two kinetic forms for Ca2+: one was a high-affinity low-capacity form; the other had a low affinity and high capacity. The Ca(2+)-ATPase activity also had two kinetic forms for ATP. All kinetic forms were inhibited by Mg2+. Vanadate, calmodulin, and R-24571 had no effects on Ca(2+)-ATPase activity. A protein doublet of Ca(2+)-dependent hydroxylamine-sensitive phosphorylated intermediates was demonstrated at 125 and 136 kDa in the purified vesicles. This doublet was not altered by addition of leupeptin throughout the purification.

Cell volume-sensitive Na+-ATPase activity in rat kidney cortex cell membranes

1988 ◽  
Vol 941 (1) ◽  
pp. 107-110 ◽  
Author(s):  
Fulgencio Proverbio ◽  
JoséA. Duque ◽  
Teresa Proverbio ◽  
Reinaldo Marín
Keyword(s):  
Atpase Activity ◽  
Cell Volume ◽  
Cell Membranes ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Cortex Cell

scholarly journals Na-pump activity in rat kidney cortex cells and its relationship with the cell volume

FEBS Letters ◽  
1988 ◽  
Vol 236 (2) ◽  
pp. 318-320 ◽  
Author(s):  
Fulgencio Proverbio ◽  
Teresa Proverbio ◽  
Rosalía G. Matteo ◽  
Trina M. Perrone ◽  
Reinaldo Marín
Keyword(s):  
Cell Volume ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Na Pump ◽  
Pump Activity

scholarly journals Ouabain-insensitive, Na+-stimulated ATPase of several rat tissues: activity during a 24 h period

2009 ◽  
pp. 693-699
Author(s):  
A Reyes ◽  
MM Galindo ◽  
L García ◽  
D Segura-Peña ◽  
C Caruso-Neves ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Blood Plasma ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Tissues ◽  
Na Transport ◽  
Rat Kidney Cortex ◽  
Low Concentrations ◽  
Two Peaks ◽  
Daily Changes

Rhythmic daily changes in the Na,K-ATPase activity have been previously described for rat kidney cortex, showing two peaks: at 0900 h and 2100 h, and two valleys: at 1500 h and 0100 h - 0300 h. The oscillations in Na,K-ATPase activity are produced by an inhibitor, which binds the enzyme and is present in the rat blood plasma at valley times and absent or at very low concentrations at peak times. Since it has been demonstrated that active Na+ extrusion from the cells of several tissues depends not only on the Na,K-ATPase but also on the ouabaininsensitive Na-ATPase, we studied the activity of this latter enzyme of several rat tissues, i.e., kidney cortex, small intestine, liver, heart and red blood cells along the day. None of these tissues showed any variation of their Na-ATPase activity along the day. Preincubation of kidney cortex homogenates obtained at 0900 h, with blood plasma drawn at 0900 h and 1500 h, did not modify the Na-ATPase activity. Our results indicate that the NaATPase activity does not oscillate along the day. These results are in agreement with the idea that the Na-ATPase could partially compensate the Na+ transport affected by oscillations of the Na,K-ATPase activity.

scholarly journals Increase of Na/Pi-cotransport encoding mRNA in response to low Pi diet in rat kidney cortex.

1994 ◽  
Vol 269 (9) ◽  
pp. 6637-6639
Author(s):  
A. Werner ◽  
S.A. Kempson ◽  
J. Biber ◽  
H. Murer
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Cytochrome P-450K of rat kidney cortex microsomes: Further studies on its interaction with fatty acids

1973 ◽  
Vol 158 (2) ◽  
pp. 597-604 ◽  
Author(s):  
Åke Ellin ◽  
Sten Orrenius ◽  
Åke Pilotti ◽  
Carl-Gunnar Swahn
Keyword(s):  
Fatty Acids ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

scholarly journals Studies on the orientation of brush-border membrane vesicles

1978 ◽  
Vol 172 (1) ◽  
pp. 57-62 ◽  
Author(s):  
W Haase ◽  
A Schäfer ◽  
H Murer ◽  
R Kinne
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Freeze Fracture ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Immunological Methods ◽  
Kidney Cortex ◽  
Asymmetric Distribution ◽  
Rat Kidney Cortex

Orientation of rat renal and intestinal brush-border membrane vesicles was studied with two independent methods: electron-microscopic freeze-fracture technique and immunological methods. With the freeze-fracture technique a distinct asymmetric distribution of particles on the two membrane fracture faces was demonstrated; this was used as a criterion for orientation of the isolated membrane vesicles. For the immunological approach the accessibility or inaccessibility of aminopeptidase M localized on the outer surface of the cell membrane to antibodies was used. With both methods we showed that the brush-border membrane vesicles isolated from rat kidney cortex and from rat small intestine for transport studies are predominantly orientated right-side out.

Endogenous Kallikrein Inhibitor in Rat Kidney Cortex-Effect of Glucocorticoid Administration

1986 ◽  
pp. 361-365 ◽  
Author(s):  
Kodo Ito ◽  
Kenichi Yamada ◽  
Setsuko Yoshida ◽  
Keiji Hasunuma ◽  
Yasushi Tamura ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Kallikrein Inhibitor ◽  
Glucocorticoid Administration
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