scholarly journals Relationship between intracellular ionic strength and expression of tonicity‐responsive genes in rat papillary collecting duct cells

2002 ◽  
Vol 543 (1) ◽  
pp. 147-153 ◽  
Author(s):  
Wolfgang Neuhofer ◽  
Helmut Bartels ◽  
Maria‐L. Fraek ◽  
Franz‐X. Beck
Keyword(s):  
Ionic Strength ◽  
Collecting Duct ◽  
Duct Cells ◽  
Papillary Collecting Duct ◽  
Collecting Duct Cells

scholarly journals A Na-K-Cl cotransporter in isolated rat papillary collecting duct cells

1989 ◽  
Vol 36 (2) ◽  
pp. 201-209 ◽  
Author(s):  
Clemens Grupp ◽  
Iris Pavenstädt-Grupp ◽  
R. Willi Grunewald ◽  
Christopher Bevan ◽  
John B. Stokes ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Duct Cells ◽  
Papillary Collecting Duct ◽  
Collecting Duct Cells ◽  
Isolated Rat

Bradykinin modulates focal adhesions and induces stress fiber remodeling in renal papillary collecting duct cells

2008 ◽  
Vol 294 (3) ◽  
pp. F603-F613 ◽  
Author(s):  
María Gabriela Márquez ◽  
María del Carmen Fernández-Tome ◽  
Nicolás Octavio Favale ◽  
Lucila Gisele Pescio ◽  
Norma Beatriz Sterin-Speziale
Keyword(s):  
Cultured Cells ◽  
Cell Attachment ◽  
Average Length ◽  
Collecting Duct ◽  
Focal Adhesions ◽  
Axial Ratio ◽  
Cytoskeleton Organization ◽  
Duct Cells ◽  
Papillary Collecting Duct ◽  
Collecting Duct Cells

Focal adhesions (FAs) are specialized regions of cell attachment to the extracellular matrix. Previous works have suggested that bradykinin (BK) can modulate cell-matrix interaction. In the present study, we used a physiological cellular model to evaluate the potential role of BK in modulating FAs and stress fibers. We performed a quantitative morphometric analysis of FAs in primary cultured rat renal papillary collecting duct cells, which included size, axial ratio (shape), and average length. After 1, 5, or 10 min of incubation with BK, cultured cells were immunostained and analyzed by confocal microscopy. Although the shape of FAs was not altered, BK induced a decrease in the number of vinculin-stained FAs per cell, and a decrease in both their size and their average length, but not in talin-containing FAs, thus suggesting that BK could be inducing a restructuring of FAs. BK also induced a remodeling of the actin filament assemblies rather than their dissipation. Since we have previously demonstrated that BK stimulates activation of PLCβ in rat renal papillae, we attempted to determine whether BK can modulate FA restructuring by this mechanism, by pretreating cultured cells with the PLCβ inhibitor U73122. The present study, performed under physiological conditions with cells that were not genetically manipulated, provides new experimental evidence supporting the notion that the intrarenal hormone BK modulates FAs and actin cytoskeleton organization through a mechanism that involves the activation of PLCβ. We propose this finding as a novel mechanism for BK modulation of tubular collecting duct function.

Detection of a Na+-H+ antiporter in cultured rat renal papillary collecting duct cells

1987 ◽  
Vol 253 (5) ◽  
pp. F889-F895 ◽  
Author(s):  
S. M. Wall ◽  
S. Muallem ◽  
J. A. Kraut
Keyword(s):  
Collecting Duct ◽  
Sodium Concentration ◽  
Significant Rise ◽  
Fluorescent Signal ◽  
Tetramethylammonium Chloride ◽  
Duct Cells ◽  
Papillary Collecting Duct ◽  
Collecting Duct Cells ◽  
High Concentrations ◽  
Extracellular Sodium

To examine whether Na+-dependent H+ transport is present in the papillary collecting duct, changes in intracellular pH (pHi) were evaluated in cultured papillary collecting duct cells acidified to a pHi of 6.3 and then placed into Na+-free or Na+-containing solutions. pHi was determined from changes in the fluorescent signal of the pH-sensitive dye BCECF. pHi did not change significantly when cells were placed in tetramethylammonium chloride- or KCl-containing solutions; however, a significant rise in pHi occurred when acid-loaded cells were placed in solutions containing 140 mM NaCl. The Na+-dependent rise in pHi was blocked by high concentrations of amiloride, but was not affected by alterations in membrane potential across the cell. The rate of rise in pHi was a function of extracellular sodium concentration with a Km for Na+ of 30 +/- 12 mM (n = 6). The properties of this Na+-dependent H+ efflux supports the presence of a Na+-H+ antiporter in the papillary collecting duct.

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P2 in renal papillary collecting duct cells

2009 ◽  
Vol 297 (5) ◽  
pp. F1181-F1191 ◽  
Author(s):  
María Gabriela Márquez ◽  
María del Carmen Fernández-Tome ◽  
Nicolás Octavio Favale ◽  
Lucila Gisele Pescio ◽  
Norma Beatriz Sterin-Speziale
Keyword(s):  
Cell Attachment ◽  
Collecting Duct ◽  
Physiological Mechanism ◽  
Focal Adhesions ◽  
Duct Cells ◽  
Cytoskeleton Reorganization ◽  
Papillary Collecting Duct ◽  
Collecting Duct Cells ◽  
Genetically Manipulated ◽  
First Time

Focal adhesions (FAs) are structures of cell attachment to the extracellular matrix. We previously demonstrated that the intrarenal hormone bradykinin (BK) induces the restructuring of FAs in papillary collecting duct cells by dissipation of vinculin, but not talin, from FAs through a mechanism that involves PLCβ activation, and that it also induces actin cytoskeleton reorganization. In the present study we investigated the mechanism by which BK induces the dissipation of vinculin-stained FAs in collecting duct cells. We found that BK induces the internalization of vinculin by a noncaveolar and independent pinocytic pathway and that at least a fraction of this protein is delivered to the recycling endosomal compartment, where it colocalizes with the transferrin receptor. Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. The present study, which was carried out with cells that were not genetically manipulated, shows for the first time that BK induces the formation of vesicle-like structures containing vinculin and PtdIns(4,5)P2, which transport vinculin to the site of FA assembly. Therefore, the modulation of the formation of these vesicle-like structures could be a physiological mechanism through which the cell can reuse the BK-induced internalized vinculin to be delivered for newly forming FAs in renal papillary collecting duct cells.

Sex difference in the antidiuretic activity of vasopressin in the rat

1993 ◽  
Vol 265 (6) ◽  
pp. R1284-R1290 ◽  
Author(s):  
Y. X. Wang ◽  
R. M. Edwards ◽  
P. Nambi ◽  
E. J. Stack ◽  
M. Pullen ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Female Rats ◽  
Camp Accumulation ◽  
Male And Female ◽  
Antidiuretic Activity ◽  
Duct Cells ◽  
Male And Female Rats ◽  
Papillary Collecting Duct ◽  
Collecting Duct Cells ◽  
Dose Dependent

A possible gender difference in the antidiuretic activity of vasopressin was studied in male and female Sprague-Dawley rats. Infusion of vasopressin (3-100 pg.kg-1.min) into conscious, chronically instrumented water-loaded rats resulted in a dose-dependent antidiuresis in both male and female rats. Male rats, however, were more than three times more sensitive to vasopressin than female rats. Thus the effective doses of vasopressin (pg.kg-1.min-1) to decrease urine flow to 30 microliters.min-1.100 g-1 (18 +/- 5 in males; 58 +/- 12 in females), to increase urine osmolality to 600 mosmol/kgH2O (35 +/- 5 in males; 119 +/- 15 in females), and to decrease free water clearance to 30 microliters.min-1.100 g-1 (8 +/- 3 in males; 28 +/- 7 in females) were significantly (P < 0.05) lower in males. Furthermore, in vitro studies in papillary collecting duct cells demonstrated a significantly higher density of vasopressin V2 receptors and a greater ability of vasopressin to stimulate adenosine 3',5'-cyclic monophosphate (cAMP) accumulation in males than in females. Vasopressin V2-receptor density (maximum binding) was 359 +/- 47 and 238 +/- 22 fmol/mg in male and female rats, respectively (P < 0.05). There was no difference in apparent dissociation constants (Kd). Vasopressin resulted in a dose-dependent increase in cAMP accumulation in papillary collecting duct cells, and at the highest concentration of vasopressin used (10(-8) M) cAMP increased from 44 +/- 10 to 182 +/- 51 fmol/micrograms protein in males and from 30 +/- 4 to 91 +/- 18 fmol/micrograms protein in females (P < 0.05). (ABSTRACT TRUNCATED AT 250 WORDS)

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