Aquaporin-3 water channel localization and regulation in rat kidney

Ecelbarger, Carolyn A.; Terris, James; Frindt, Gustavo; Echevarría, Miriam; Marples, David; Nielsen, Søren; Knepper, Mark A.

doi:10.1152/ajprenal.1995.269.5.f663

Cited by 280 publications

(320 citation statements)

References 16 publications

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“…[21][22][23] Kidneys from control and acidosis rats were homogenized in an ice-cold isolation solution (10 mM triethanolamine (pH 7.6) and 250 mM sucrose) containing protease inhibitors, leupeptin (1 mg ml À1 ; Peptide Institute, Osaka, Japan) and phenylmethylsulfonyl fluoride (0.1 mg ml À1 ; Wako Pure Chemical, Tokyo, Japan), some of which were collected as whole-kidney homogenates. The remainders were centrifuged initially at 4000 g for 10 min at 4 1C (Himac centrifuge CR5B, Hitachi, Tokyo, Japan) to remove incompletely homogenized fragments and nuclei.…”

Section: Differential Centrifugationmentioning

confidence: 99%

Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts

et al. 2009

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Renal aquaporin-2 (AQP2) expression plays a key role in urine concentration. However, it is not known whether metabolic acidosis affects urine-concentrating ability through AQP2 expression in the kidney and urine. We examined urinary excretion and renal expression of AQP2 in control and acidosis rats, using RT-competitive PCR, immunoblot and immunocytochemistry. Urinary excretion of AQP2 is decreased by 92% even with the increase in AQP2 mRNA and protein expressions in the collecting ducts by metabolic acidosis in rats. Urine osmolality in control rats was 1670 ± 198 mOsm per kg H 2 O, and immunocytochemistry revealed the presence of AQP2 in the apical plasma membrane of the principal cells in the collecting ducts. Urine osmolality in acidosis rats was lower than that in control (1397±243 mOsm per kg H 2 O), and immunocytochemistry showed the diffuse presence of AQP2 in the cytoplasm of the principal cells. Differential centrifugationcoupled immunoblot showed a significant decrease in the ratio of AQP2 in plasma membrane-enriched fraction to that in intracellular vesicle-enriched fraction by metabolic acidosis. In summary, AQP2 translocation is largely decreased by metabolic acidosis even with increased expression in the collecting ducts. A disorder of AQP2 translocation in the collecting ducts with acidosis may be responsible for the diuresis in patients with chronic renal failure.

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Section: Differential Centrifugationmentioning

confidence: 99%

Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts

et al. 2009

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“…The existence of independent water and glycerol transporting domains was suggested by one group of scientists; the existence of a single pore was suggested by a second group; a third group incorrectly reported that the molecule was impermeable to water. The abundant expression of AQP3 at the basolateral membranes of principal cells in the collecting duct suggests a role in renal water reabsorption (37). AQP3 is also expressed in multiple other tissues including airways and is particularly abundant in nasopharyngeal epithelium, where roles in mucosal secretions and allergic rhinitis are suspected (32).…”

Section: Minireview: Aquaporins Blueprints For Cellular Plumbing Sysmentioning

confidence: 99%

“…These aquaporins presumably function together to provide transcellular water flow. In principal cells of the collecting duct, AQP2 is shuttled to the apical membrane permitting water entry from the lumen, whereas AQP3 and AQP4 reside at the basolateral membranes providing exit ports to the interstitium (37,40). Pulmonary tissues develop a large capacity for fluid absorption in the perinatal state and provide humidification of the airways and airway secretions (see Ref.…”

Section: Multiple Aquaporins In Complex Tissuesmentioning

confidence: 99%

The Aquaporins, Blueprints for Cellular Plumbing Systems

Agre

Bonhivers²,

Borgnia³

1998

Journal of Biological Chemistry

422

281

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Membrane Water PermeabilityPlasma membranes provide an effective barrier to the extracellular environment. Water was long believed to move through lipid bilayers by simple diffusion; however, membranes from different tissues vary in their permeability to water. The variability is particularly evident in mammalian kidney where proximal tubules and descending thin limbs of Henle's loop have constitutively high water permeability and are responsible for reabsorption of more than 150 liters per day in adult humans. In contrast, ascending thin limbs have very low water permeability. Renal distal tubules empty into collecting ducts where stimulation with vasopressin causes an increase in water permeability (see Ref. 1 for review). These observations led to the suggestion that specialized water transport molecules must exist in membranes with intrinsically high water permeability. Nevertheless, despite extensive studies, the molecular identity of water transport proteins remained elusive until recently.The well defined features of membrane water permeability permitted serendipitous identification of the first known water channel. While purifying the 32-kDa subunit of the red cell Rh blood group antigen, a new 28-kDa polypeptide was discovered (2). Detailed biochemical studies of this newly identified tetrameric membrane protein were made easy by its low solubility in N-lauroylsarcosine, which permitted simple purification (3). The abundance of the protein in rat renal proximal tubules and descending thin limbs (2) sparked the idea that the 28-kDa polypeptide may be the long sought water channel, and its unique N-terminal amino acid sequence permitted cloning from an erythroid cDNA library (4). Functional Analyses of AQP1The Xenopus oocyte expression system has been extremely useful for study of water transport. Oocytes injected with cRNA for the 28-kDa polypeptide exhibit remarkably high osmotic water permeability (P f ϳ200 ϫ 10 Ϫ4 cm s Ϫ1) and rapidly explode in hypotonic buffer (Fig. 1), whereas control oocytes exhibit minimal permeability (5). First referred to as "CHIP28," this protein is now designated aquaporin-1 (AQP1) 1 by the Human Genome Nomenclature Committee (see http://www.gene.ucl.ac.uk/nomenclature). Despite its large water permeability, AQP1 failed to confer a measurable increase in membrane currents (5). Consistent with these results, highly purified AQP1 protein reconstituted into proteoliposomes exhibits high unit water permeability (P f ϳ3 ϫ 10 9 water molecules subunit Ϫ1 s Ϫ1 ), whereas permeation by other small solutes or even protons was undetectable (6). The prevailing view is that AQP1 is a constitutively active, water-selective pore that permits osmotically driven movement of water. A report that forskolin induces a cation current in AQP1-expressing oocytes (7) was not reproduced by multiple other scientific groups. Permeation by CO 2 has recently been proposed, because rates of pH change are about 40% higher in oocytes expressing AQP1 (8). Permeation by O 2 , nitric oxide, and other gases is...

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“…In rat, AQP3 protein is constitutively expressed on basolateral membranes of principal cells in cortical and outer medullary collecting duct (8,9,14,15). AQP4 protein is also expressed at the basolateral membrane of collecting-duct epithelial cells but mostly in inner medullary collecting-duct segments (9,16).…”

mentioning

confidence: 99%

Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels

Song

Yang

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

362

251

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Aquaporin-3 (AQP3) is a water channel expressed at the basolateral plasma membrane of kidney collecting-duct epithelial cells. The mouse AQP3 cDNA was isolated and encodes a 292-amino acid water͞glycerol-transporting glycoprotein expressed in kidney, large airways, eye, urinary bladder, skin, and gastrointestinal tract. The mouse AQP3 gene was analyzed, and AQP3 null mice were generated by targeted gene disruption. The growth and phenotype of AQP3 null mice were grossly normal except for polyuria. AQP3 deletion had little effect on AQP1 or AQP4 protein expression but decreased AQP2 protein expression particularly in renal cortex. Fluid consumption in AQP3 null mice was more than 10-fold greater than that in wild-type litter mates, and urine osmolality (<275 milliosmol) was much lower than in wild-type mice (>1,200 milliosmol). After 1-desamino-8-D-arginine-vasopressin administration or water deprivation, the AQP3 null mice were able to concentrate their urine partially to Ϸ30% of that in wild-type mice. Osmotic water permeability of cortical collecting-duct basolateral membrane, measured by a spatial filtering optics method, was >3-fold reduced by AQP3 deletion. To test the hypothesis that the residual concentrating ability of AQP3 null mice was due to the inner medullary collecting-duct water channel AQP4, AQP3͞AQP4 double-knockout mice were generated. The double-knockout mice had greater impairment of urinary-concentrating ability than did the AQP3 single-knockout mice. Our findings establish a form of nephrogenic diabetes insipidus produced by impaired water permeability in collecting-duct basolateral membrane. Basolateral membrane aquaporins may thus provide blood-accessible targets for drug discovery of aquaretic inhibitors.water transport ͉ AQP3 ͉ kidney ͉ urinary-concentrating mechanism ͉ polyuria A quaporin-3 (AQP3, originally called glycerol intrinsic protein, GLIP, based on its glycerol-transport function) was cloned from rat kidney by our laboratory (1) as well as by Ishibashi et al. (2) and Echevarria et al. (3). AQP3 is a relatively weak transporter of water but functions as an efficient glycerol transporter (4). Reflection coefficient measurements (5) and mutagenesis studies (6) suggested that water and glycerol share a common pathway through the AQP3 protein, although inhibition experiments were interpreted as suggesting different pathways (7). Immunocytochemistry in rat showed AQP3 protein expression in basolateral membrane of kidney collecting duct and large airways, as well as in several tissues that are thought not to have an important water-transporting role including urinary bladder, conjunctiva, and epidermis (8-11). Recent studies report strong AQP3 expression in various regions of the gastrointestinal tract including small intestine (12). Another unique feature of AQP3 is its gene structure, which is different from the water-selective mammalian aquaporins (13). AQP3, AQP7, and AQP9 have been called ''aquaglyceroporins'' because of their relatively broad solute specificity and sequence ho...

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Aquaporin-3 water channel localization and regulation in rat kidney

Cited by 280 publications

References 16 publications

Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts

Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts

The Aquaporins, Blueprints for Cellular Plumbing Systems

Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels

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