Expression of Aquaporin-1 in the Peritoneal Tissues: Localization and Regulation by Hyperosmolality

2002 ◽  
Vol 22 (3) ◽  
pp. 307-315 ◽  
Author(s):  
Tomoko Ota ◽  
Michio Kuwahara ◽  
Shuling Fan ◽  
Yoshio Terada ◽  
Takashi Akiba ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Water Permeability ◽  
Water Channel ◽  
Mesothelial Cells ◽  
Scattering Method ◽  
Osmotic Water Permeability ◽  
Peritoneal Mesothelial Cells ◽  
Aquaporin 1 ◽  
Osmotic Water ◽  
Aqp1 Expression

Objective The purpose of this study was to determine the localization of the aquaporin-1 (AQP1) water channel in peritoneal tissues and the effect of hyperosmolality on the peritoneal expression and function of AQP1. Methods Immunohistochemical localization of AQP1 was identified in rat peritoneal tissues. Cultured rat peritoneal mesothelial cells (RPMCs) were exposed to hyperosmolality by adding 4% glucose to the culture medium. After 1 hour, 4 hours, 24 hours, and 48 hours, AQP1 was identified by semiquantitative immunoblot and immunocytochemistry. Osmotic water permeability was measured using a light-scattering method. Results Immunohistochemistry of rat peritoneal tissues showed the presence of AQP1 in mesothelial cells, venular endothelial cells, and capillary endothelial cells, but not in arteriole and interstitial cells. Semiquantitative immunoblot revealed that exposure to hyperosmolality significantly increased AQP1 expression after 24 hours in whole RPMC lysates (3.3-fold at 24 hours and 3.9-fold at 48 hours). Consistent with the immunoblot, osmotic water permeability of RPMC was augmented 1.7-fold and 2.7-fold after 1 hour and 24 hours, respectively, in a hyperosmotic environment. In RPMC membrane fractions, AQP1 expression was significantly increased after 1 hour of exposure to hyperosmolality (3.9-fold at 1 hour, 7.1-fold at 4 hours, and 8.7-fold at 24 hours). Immunocytochemistry of RPMCs showed that AQP1 was gradually redistributed from the perinuclear area to the peripheral cytoplasm, and then to the plasma membrane after a 1-hour hyperosmotic challenge, suggesting hyperosmolality-induced translocation of AQP1. Upregulation of AQP1 was also observed in the omentum of rats loaded intraperitoneally with hyperosmotic dialysate every day for 10 weeks. Conclusion AQP1 is widely distributed in the peritoneal cavity and may provide the major aqueous pathway across the peritoneal barrier. In addition, our findings suggested that hyperosmolality increases AQP1-dependent water permeability in peritoneal tissues by regulating the translocation and synthesis of AQP1 protein.

Expression of Aquaporin-1 in Human Peritoneal Mesothelial Cells and Its Upregulation by GlucoseIn Vitro

2001 ◽  
Vol 12 (5) ◽  
pp. 1036-1045 ◽  
Author(s):  
KAR NENG LAI ◽  
FU KEUNG LI ◽  
HAO YUI LAN ◽  
SYDNEY TANG ◽  
ANITA W. L. TSANG ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Peritoneal Dialysis ◽  
Mesothelial Cells ◽  
Dependent Manner ◽  
Peritoneal Membrane ◽  
Dialysis Adequacy ◽  
Peritoneal Mesothelial Cells ◽  
Aqp1 Expression ◽  
Human Peritoneal Mesothelial Cells ◽  
Osmotic Agents

Abstract. Aquaporin (AQP) is a family of water channels that are highly selective for the passage of water and occasionally glycerol. In previous studies, only AQP1 was found in human peritoneal endothelial cells in both control subjects and patients on peritoneal dialysis. As human peritoneal mesothelial cells (HPMC) play an important role in dialysis adequacy and fluid balance in continuous ambulatory peritoneal dialysis patients, this study examined whether AQP1 is present in HPMC. It was found that AQP1 mRNA and protein are present in HPMC constitutively. The localization of AQP1 protein in peritoneal mesothelial cells was confirmed by double immunohistochemical staining of the mesothelial lining of human peritoneal membrane. More important, the expression of AQP1 in HPMC is not constitutive and the transcription and biosynthesis of AQP1 in HPMC is inducible by osmotic agents such as glucose and mannitol. There was significant enhancement of AQP1 biosynthesis upon exposure to glucose in a time- and dose-dependent manner (P< 0.0001). Similar findings were observed in the AQP1 biosynthesis by an endothelial cell line, EA.hy 926. Of particular interest, the upregulation in AQP1 mRNA or biosynthesis in mesothelial cells was always significantly higher than that of endothelial cells when the experiments were conducted under identical settings (P< 0.001). AQP1 expression in HPMC was demonstrated for the first time. Osmotic agents upregulate both mRNA and protein expression of this aquaporin. The role of AQP1 in HPMC in maintaining the ultrafiltration of the peritoneal membrane is potentially of clinical interest.

Acetazolamide inhibits osmotic water permeability by interaction with aquaporin-1

2006 ◽  
Vol 350 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Junwei Gao ◽  
Xiaohua Wang ◽  
Yongjie Chang ◽  
Jianzhao Zhang ◽  
Qianliu Song ◽  
...  
Keyword(s):  
Water Permeability ◽  
Osmotic Water Permeability ◽  
Aquaporin 1 ◽  
Osmotic Water

scholarly journals Expression of multiple water channel activities in Xenopus oocytes injected with mRNA from rat kidney.

1993 ◽  
Vol 101 (6) ◽  
pp. 827-841 ◽  
Author(s):  
M Echevarria ◽  
G Frindt ◽  
G M Preston ◽  
S Milovanovic ◽  
P Agre ◽  
...  
Keyword(s):  
Water Permeability ◽  
Antisense Oligonucleotide ◽  
Xenopus Oocytes ◽  
Rat Kidney ◽  
Water Channel ◽  
Water Channels ◽  
Renal Tissue ◽  
Osmotic Water Permeability ◽  
Volume Increase ◽  
Osmotic Water

To test the hypothesis that renal tissue contains multiple distinct water channels, mRNA prepared from either cortex, medulla, or papilla of rat kidney was injected into Xenopus oocytes. The osmotic water permeability (Pf) of oocytes injected with either 50 nl of water or 50 nl of renal mRNA (1 microgram/microliter) was measured 4 d after the injection. Pf was calculated from the rate of volume increase on exposure to hyposmotic medium. Injection of each renal mRNA preparation increased the oocyte Pf. This expressed water permeability was inhibited by p-chloromercuriphenylsulfonate and had a low energy of activation, consistent with the expression of water channels. The coinjection of an antisense oligonucleotide for CHIP28 protein, at an assumed &gt; 100-fold molar excess, with either cortex, medulla, or papilla mRNA reduced the expression of the water permeability by approximately 70, 100, and 30%, respectively. Exposure of the oocyte to cAMP for 1 h resulted in a further increase in Pf only in oocytes injected with medulla mRNA. This cAMP activation was not altered by the CHIP28 antisense oligonucleotide. These results suggest that multiple distinct water channels were expressed in oocytes injected with mRNA obtained from sections of rat kidney: (a) CHIP28 water channels in cortex and medulla, (b) cAMP-activated water channels in medulla, and (c) cAMP-insensitive water channels in papilla.

scholarly journals Relative CO2/NH3 selectivities of mammalian aquaporins 0–9

2013 ◽  
Vol 304 (10) ◽  
pp. C985-C994 ◽  
Author(s):  
R. Ryan Geyer ◽  
Raif Musa-Aziz ◽  
Xue Qin ◽  
Walter F. Boron
Keyword(s):  
Plasma Membrane ◽  
Water Permeability ◽  
Xenopus Oocytes ◽  
Video Microscopy ◽  
Osmotic Water Permeability ◽  
Permeability Ratio ◽  
Diverse Range ◽  
Surface Ph ◽  
Aquaporin 1 ◽  
Osmotic Water

Previous work showed that aquaporin 1 (AQP1), AQP4-M23, and AQP5 each has a characteristic CO2/NH3 and CO2/H2O permeability ratio. The goal of the present study is to characterize AQPs 0–9, which traffic to the plasma membrane when heterologously expressed in Xenopus oocytes. We use video microscopy to compute osmotic water permeability ( Pf) and microelectrodes to record transient changes in surface pH (ΔpHS) caused by CO2 or NH3 influx. Subtracting respective values for day-matched, H2O-injected control oocytes yields the channel-specific values Pf* and ΔpHS*. We find that Pf* is significantly >0 for all AQPs tested except AQP6. (ΔpHS*)CO2 is significantly >0 for AQP0, AQP1, AQP4-M23, AQP5, AQP6, and AQP9. (ΔpHS*)NH3 is >0 for AQP1, AQP3, AQP6, AQP7, AQP8, and AQP9. The ratio (ΔpHS*)CO2/ Pf* falls in the sequence AQP6 (∞) > AQP5 > AQP4-M23 > AQP0 ≅ AQP1 ≅ AQP9 > others (0). The ratio (ΔpHS*)NH3/ Pf* falls in the sequence AQP6 (∞) > AQP3 ≅ AQP7 ≅ AQP8 ≅ AQP9 > AQP1 > others (0). Finally, the ratio (ΔpHS*)CO2/(−ΔpHS*)NH3 falls in the sequence AQP0 (∞) ≅ AQP4-M23 ≅ AQP5 > AQP6 > AQP1 > AQP9 > AQP3 (0) ≅ AQP7 ≅ AQP8. The ratio (ΔpHS*)CO2/(−ΔpHS*)NH3 is indeterminate for both AQP2 and AQP4-M1. In summary, we find that mammalian AQPs exhibit a diverse range of selectivities for CO2 vs. NH3 vs. H2O. As a consequence, by expressing specific combinations of AQPs, cells could exert considerable control over the movements of each of these three substances.

Unimpaired osmotic water permeability and fluid secretion in bile duct epithelia of AQP1 null mice

2002 ◽  
Vol 283 (3) ◽  
pp. G739-G746 ◽  
Author(s):  
Albert Mennone ◽  
Alan S. Verkman ◽  
James L. Boyer
Keyword(s):  
Bile Duct ◽  
Cyclic Amp ◽  
Water Permeability ◽  
Water Movement ◽  
Fluid Secretion ◽  
Osmotic Gradient ◽  
Osmotic Water Permeability ◽  
Luminal Membrane ◽  
Osmotic Water ◽  
Aqp1 Expression

The mechanisms by which fluid moves across the luminal membrane of cholangiocyte epithelia are uncertain. Previous studies suggested that aquaporin-1 (AQP1) is an important determinant of water movement in rat cholangiocytes and that cyclic AMP mediates the movement of these water channels from cytoplasm to apical membrane, thereby increasing the osmotic water permeability. To test this possibility we measured agonist-stimulated fluid secretion and osmotically driven water transport in isolated bile duct units (IBDUs) from AQP1 wild-type (+/+) and null (−/−) mice. AQP1 expression was confirmed in a mouse cholangiocyte cell line and +/+ liver. Forskolin-induced fluid secretion, measured from the kinetics of IBDU luminal expansion, was 0.05 fl/min and was not impaired in −/− mice. Osmotic water permeability (Pf), measured from the initial rate of IBDU swelling in response to a 70-mosM osmotic gradient, was 11.1 × 10−4 cm/s in +/+ mice and 11.5 × 10−4cm/s in −/− mice. Pf values increased by ∼50% in both +/+ and −/− mice following preincubation with forskolin. These findings provide direct evidence that AQP1 is not rate limiting for water movement in mouse cholangiocytes and does not appear to be regulated by cyclic AMP in this species.

Functional analysis of aquaporin-2 mutants associated with nephrogenic diabetes insipidus by yeast expression

1999 ◽  
Vol 277 (5) ◽  
pp. F734-F741 ◽  
Author(s):  
Itsuki Shinbo ◽  
Kiyohide Fushimi ◽  
Michihiro Kasahara ◽  
Kazushi Yamauchi ◽  
Sei Sasaki ◽  
...  
Keyword(s):  
Diabetes Insipidus ◽  
Water Permeability ◽  
Nephrogenic Diabetes Insipidus ◽  
Water Channel ◽  
Osmotic Water Permeability ◽  
Wild Type ◽  
The Third ◽  
Aquaporin 2 ◽  
Channel Water ◽  
Osmotic Water

Mutations of aquaporin-2 (AQP2) vasopressin water channel cause nephrogenic diabetes insipidus (NDI). It has been suggested that impaired routing of AQP2 mutants to the plasma membrane causes the disease; however, no determinations have been made of mutation-induced alterations of AQP2 channel water permeability. To address this issue, a series of AQP2 mutants were expressed in yeast, and the osmotic water permeability ( Pf) of the isolated vesicles was measured. Wild-type and mutant AQP2 were expressed equally well in vesicles. Pfof the vesicles containing wild-type AQP2 was 22 times greater than that of the control, which was sensitive to mercury and weakly dependent on the temperature. Pfmeasurements and mercury inhibition examinations suggested that mutants L22V and P262L are fully functional, whereas mutants N68S, R187C, and S216P are partially functional. In contrast, mutants N123D, T125M, T126M, A147T, and C181W had very low water permeability. Our results suggest that the structure between the third and fifth hydrophilic loops is critical for the functional integrity of the AQP2 water channel and that disruption of AQP2 water permeability by mutations may cause NDI.

Osmotic water permeability of aquaporin-1 under radial tensile and compressive stimuli

Desalination ◽  
2020 ◽  
Vol 492 ◽  
pp. 114524
Author(s):  
Shaghayegh Bahari ◽  
Reza Davarnejad ◽  
Omid Bavi ◽  
Seyed Vahid Mohammadi
Keyword(s):  
Water Permeability ◽  
Osmotic Water Permeability ◽  
Aquaporin 1 ◽  
Osmotic Water
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