Effect of ?high ceiling? diuretics on active salt transport in the cortical thick ascending limb of Henle's loop of rabbit kidney

1983 ◽  
Vol 396 (3) ◽  
pp. 210-217 ◽  
Author(s):  
E. Schlatter ◽  
R. Greger ◽  
C. Weidtke
Keyword(s):  
Salt Transport ◽  
Rabbit Kidney ◽  
Thick Ascending Limb ◽  
Henle's Loop ◽  
Active Salt

Distribution and diversity of Na-K-Cl cotransport proteins: a study with monoclonal antibodies

1995 ◽  
Vol 269 (6) ◽  
pp. C1496-C1505 ◽  
Author(s):  
C. Lytle ◽  
J. C. Xu ◽  
D. Biemesderfer ◽  
B. Forbush
Keyword(s):  
Monoclonal Antibodies ◽  
Loop Diuretic ◽  
Chloride Secretion ◽  
Salt Transport ◽  
Rabbit Kidney ◽  
Thick Ascending Limb ◽  
Animal Cells ◽  
Immunoreactive Protein ◽  
Site Density ◽  
Carboxy Terminal

The Na-K-Cl cotransporter (NKCC) is present in most animal cells where it functions in cell volume homeostasis and epithelial salt transport. We developed six monoclonal antibodies (designated T4, T8, T9, T10, T12, and T14) against a fusion protein fragment encompassing the carboxy-terminal 310 amino acids of the human colonic NKCC. These T antibodies selectively recognized putative NKCC proteins in a diverse variety of animal tissues. Western blot analysis of membranes isolated from 23 types of cells identified single bands of immunoreactive protein ranging in mass from 146 to 205 kDa. The amount of immunoreactive protein detected in these cells correlated with loop diuretic binding site density. Proteins identified previously as Na-K-Cl cotransporters by loop diuretic photoaffinity labeling were mutually recognized by multiple T antibodies. Most of the T antibodies effectively immunoprecipitated the denatured form of the NKCC protein. Immunocytochemical studies on the rabbit parotid gland demonstrated that NKCC is restricted to the basolateral margin of the acinar cells and absent from the ducts, in accord with the central role of Na-K-Cl cotransport in chloride secretion. In the rabbit kidney, NKCC was localized to the apical membrane of thick ascending limb cells, consistent with its role in chloride reabsorption.

Characterization of Aldose Reductase from the Thick Ascending Limb of Henle’s Loop of Rabbit Kidney

Nephron ◽  
2001 ◽  
Vol 89 (1) ◽  
pp. 73-81 ◽  
Author(s):  
R. Willi Grunewald ◽  
Angela Eckstein ◽  
Claudius H. Reisse ◽  
Gerhard A. Müller
Keyword(s):  
Aldose Reductase ◽  
Rabbit Kidney ◽  
Thick Ascending Limb ◽  
Henle's Loop

Effect of high protein intake on sodium, potassium-dependent adenosine triphosphatase activity in the thick ascending limb of Henle's loop in the rat

1988 ◽  
Vol 74 (3) ◽  
pp. 319-329 ◽  
Author(s):  
Nadine Bouby ◽  
Lise Bankir
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Unit Length ◽  
High Protein Diet ◽  
High Protein ◽  
Salt Transport ◽  
Protein Diet ◽  
Thick Ascending Limb ◽  
Sodium Potassium ◽  
Henle's Loop

1. We have previously shown that the hypertrophy of the kidney induced by a high protein diet consists of a preferential hypertrophy of the thick ascending limb (TAL) of Henle's loop. This might be related to an increase in the active salt transport by this segment. Sodium, potassium-dependent adenosine triphosphatase (Na+,K+-ATPase) activity was measured in TAL from kidneys of rats fed either a low (LP) or a high (HP) protein diet for several weeks. 2. Enzymatic activity was measured by microdensitometry, after appropriate cytochemical reaction, for an adenosine 5′-triphosphate (ATP) concentration of 0–66 mmol/l. Both activity per unit tubular length and mean activity per unit tissue volume were recorded. A calibration was designed to convert usual microdensitometry units (extinction) into conventional biochemical units (mol of product formed). 3. For non-limiting substrate concentrations, the Na+,K+-ATPase activity, expressed per unit length of tubule on the sections, was 50% higher in HP than in LP rats, an increase proportional to that of the simultaneously measured tubule diameter. When expressed per unit tubular volume, Na+,K+-ATPase activity was similar in both groups of rats. The dissociation constant for ATP was also similar in both groups. 4. Results show that a high protein diet induces an increase in Na+,K+-ATPase activity in TAL, thus enabling an enhanced NaCl transport in this segment. This increase in transport capacity is not due to an increase in the density of enzymatic units but to an increase in their number, in relation to the hypertrophy of the TAL.

A potassium channel in the apical membrane of rabbit thick ascending limb of Henle's loop

1990 ◽  
Vol 258 (2) ◽  
pp. F244-F253 ◽  
Author(s):  
W. H. Wang ◽  
S. White ◽  
J. Geibel ◽  
G. Giebisch
Keyword(s):  
Apical Membrane ◽  
Rabbit Kidney ◽  
K Channel ◽  
Thick Ascending Limb ◽  
Dependent Manner ◽  
Patch Clamp Technique ◽  
Bath Solution ◽  
Henle's Loop ◽  
Voltage Dependent ◽  
Inside Out

We used the patch-clamp technique to study the activity of single potassium channels in the apical membrane of isolated thick ascending limbs of Henle's loop (TAL) of rabbit kidneys. In cell-attached patches with NaCl Ringer or high-K+ solution in the bath and 140 mM K+ in the pipette, an inwardly rectifying K+ channel was observed with an inward slope conductance of 22.0 +/- 0.5 pS and outward slope conductance of 10.2 +/- 0.3 pS at 22 degrees C (n = 15). The channel was highly selective for K+, with a calculated permeability ratio for K(+)-to-Na+ of 20:1 (n = 4). The open probability (Po) of the channel was 0.89 +/- 0.03 (n = 15) and was not voltage dependent. In inside-out patches with 140 mM K+ in both the bath and the pipette solutions, both Po and conductance of the channel were similar to that in cell-attached patches. Addition of 0.1 mM Ba2+ to the pipette solution reduced Po of the channel in a voltage-dependent manner. Lowering the pH of the bath solution from 7.4 to 6.9 or increasing Ca2+ concentration from 0 to 0.5 mM in inside-out patches did not alter either Po or conductance of the channel. Addition of 2 mM ATP to the bath solution completely inhibited channel activity. This ATP-induced inhibition was fully reversible and was found to be dependent on the ratio of ATP to ADP, since adding 1 mM ADP to the bath solution relieved the ATP-induced blockade. The property of this small-conductance K+ channel make it a likely candidate for recycling of K+ across the apical membrane of TAL of the rabbit kidney. ATP and ADP are possible intracellular regulators of the channel's activity.

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