Effect on stability, degradation, expression, and targeting of aquaporin-2 water channel by hyperosmolality in renal epithelial cells

2005 ◽  
Vol 338 (3) ◽  
pp. 1593-1599 ◽  
Author(s):  
Fuminori Umenishi ◽  
Takefumi Narikiyo ◽  
Robert W. Schrier
2002 ◽  
Vol 278 (2) ◽  
pp. 1101-1107 ◽  
Author(s):  
Bas W. M. van Balkom ◽  
Marcel van Raak ◽  
Sylvie Breton ◽  
Nuria Pastor-Soler ◽  
Richard Bouley ◽  
...  

Cells ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 1057
Author(s):  
Richard Bouley ◽  
Naofumi Yui ◽  
Abby Terlouw ◽  
Pui W. Cheung ◽  
Dennis Brown

We previously showed that in polarized Madin–Darby canine kidney (MDCK) cells, aquaporin-2 (AQP2) is continuously targeted to the basolateral plasma membrane from which it is rapidly retrieved by clathrin-mediated endocytosis. It then undertakes microtubule-dependent transcytosis toward the apical plasma membrane. In this study, we found that treatment with chlorpromazine (CPZ, an inhibitor of clathrin-mediated endocytosis) results in AQP2 accumulation in the basolateral, but not the apical plasma membrane of epithelial cells. In MDCK cells, both AQP2 and clathrin were concentrated in the basolateral plasma membrane after CPZ treatment (100 µM for 15 min), and endocytosis was reduced. Then, using rhodamine phalloidin staining, we found that basolateral, but not apical, F-actin was selectively reduced by CPZ treatment. After incubation of rat kidney slices in situ with CPZ (200 µM for 15 min), basolateral AQP2 and clathrin were increased in principal cells, which simultaneously showed a significant decrease of basolateral compared to apical F-actin staining. These results indicate that clathrin-dependent transcytosis of AQP2 is an essential part of its trafficking pathway in renal epithelial cells and that this process can be inhibited by selectively depolymerizing the basolateral actin pool using CPZ.


2020 ◽  
Vol 21 (12) ◽  
pp. 4288
Author(s):  
Ahmed Abdeen ◽  
Hiroko Sonoda ◽  
Ayaha Kaito ◽  
Sayaka Oshikawa-Hori ◽  
Naruki Fujimoto ◽  
...  

Urinary exosomes, small extracellular vesicles present in urine, are secreted from all types of renal epithelial cells. Aquaporin-2 (AQP2), a vasopressin-regulated water channel protein, is known to be selectively excreted into the urine through exosomes (UE-AQP2), and its renal expression is decreased in nephrotic syndrome. However, it is still unclear whether excretion of UE-AQP2 is altered in nephrotic syndrome. In this study, we examined the excretion of UE-AQP2 in an experimental rat model of nephrotic syndrome induced by the administration of puromycin aminonucleoside (PAN). Rats were assigned to two groups: a control group administered saline and a PAN group given a single intraperitoneal injection of PAN (125 mg/kg) at day 0. The experiment was continued for 8 days, and samples of urine, blood, and tissue were collected on days 2, 5, and 8. The blood and urine parameters revealed that PAN induced nephrotic syndrome on days 5 and 8, and decreases in the excretion of UE-AQP2 were detected on days 2 through 8 in the PAN group. Immunohistochemistry showed that the renal expression of AQP2 was decreased on days 5 and 8. The release of exosomal marker proteins into the urine through UEs was decreased on day 5 and increased on day 8. These data suggest that UE-AQP2 is decreased in PAN-induced nephrotic syndrome and that this reflects its renal expression in the marked proteinuria phase after PAN treatment.


2000 ◽  
Vol 106 (9) ◽  
pp. 1115-1126 ◽  
Author(s):  
Richard Bouley ◽  
Sylvie Breton ◽  
Tian-xiao Sun ◽  
Margaret McLaughlin ◽  
Ndona N. Nsumu ◽  
...  

EMBO Reports ◽  
2003 ◽  
Vol 4 (1) ◽  
pp. 88-93 ◽  
Author(s):  
Dorothea Lorenz ◽  
Andrey Krylov ◽  
Daniel Hahm ◽  
Volker Hagen ◽  
Walter Rosenthal ◽  
...  

2001 ◽  
Vol 281 (3) ◽  
pp. G856-G863 ◽  
Author(s):  
Pedro Gallardo ◽  
L. Pablo Cid ◽  
Carlos P. Vio ◽  
Francisco V. Sepúlveda

Aquaporin-2 (AQP-2) is the vasopressin-regulated water channel expressed in the apical membrane of principal cells in the collecting duct and is involved in the urinary concentrating mechanism. In the rat distal colon, vasopressin stimulates water absorption through an unknown mechanism. With the hypothesis that AQP-2 could contribute to this vasopressin effect, we studied its presence in rat colonic epithelium. We used RT-PCR, in situ hybridization, immunoblotting, and immunocytochemistry to probe for AQP-2 expression. An AQP-2 amplicon was obtained through RT-PCR of colon epithelium RNA, and in situ hybridization revealed AQP-2 mRNA in colonic crypts and, to a lesser extent, in surface absorptive epithelial cells. AQP-2 protein was localized to the apical membrane of surface absorptive epithelial cells, where it colocalized with H+-K+-ATPase but not with Na+-K+-ATPase. AQP-2 was absent from the small intestine, stomach, and liver. Water deprivation increased the hybridization signal and the protein level (assessed by Western blot analysis) for AQP-2 in distal colon. This was accompanied by increased p-chloromercuriphenylsulfonic acid-sensitive water absorption. These results indicate that AQP-2 is present in the rat distal colon, where it might be involved in a water-sparing mechanism. In addition, these results support the idea that AQP-2, and probably other aquaporins, are involved in water absorption in the colon.


Author(s):  
Giuseppe Procino ◽  
Monica Carmosino ◽  
Lorenzo A. Pinna ◽  
Ildo Nicoletti ◽  
Søren Nielsen ◽  
...  

2008 ◽  
Vol 283 (39) ◽  
pp. 26643-26661 ◽  
Author(s):  
Udo Hasler ◽  
Paula Nunes ◽  
Richard Bouley ◽  
Hua A. J. Lu ◽  
Toshiyuki Matsuzaki ◽  
...  

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