At Physiological Expression Levels the Kidd Blood Group/Urea Transporter Protein Is Not a Water Channel

Sidoux-Walter, Frédéric; Lucien, Nicole; Olivès, Bernadette; Gobin, Renée; Rousselet, Germain; Kamsteeg, Erik‐Jan; Ripoche, Pierre; Deen, Peter M.T.; Cartron, Jean‐Pierre; Bailly, Pascal

doi:10.1074/jbc.274.42.30228

Cited by 67 publications

(58 citation statements)

References 35 publications

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“…Their conclusions were based upon expression studies in Xenopus laevis oocytes combined with volumetric measurements of water uptake at 10°C and [ 14 C]urea uptake at 1mmoll -1 at 23°C. Sidoux-Walter et al (Sidoux-Walter et al, 1999) questioned the conclusion by Yang and Verkman (Yang and Verkman, 1998). They showed that expression at high levels of the human RBC UT-B in Xenopus laevis oocytes induced not only high P urea and P f as reported by Yang and Verkman (Yang and Verkman, 1998), but also an increased permeability to small solutes, such as formamide through propionamide, and to diols, such as ethylene glycol and propylene glycol.…”

Section: Do Urea and Water Share A Pathway In Common In Rbc?mentioning

confidence: 69%

“…The data indicate that the transport specificity disappeared at a high level of expression. In contrast, expression at physiological levels increased (as expected) the phloretin-sensitive urea transport with no increase of P f (Sidoux-Walter et al, 1999). A study by Lucien et al (Lucien et al, 2002) also pointed out that expression of a recombinant urea transporter (hUT-B1) in Xenopus oocytes creates a P urea that is efficiently inhibited by phloretin, but much less inhibited by PCMBS than the native P urea in human RBC.…”

Section: Do Urea and Water Share A Pathway In Common In Rbc?mentioning

confidence: 98%

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The permeability of red blood cells to chloride, urea, and water

Brahm

2013

Journal of Experimental Biology

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SUMMARYThis study extends permeability (P) data on chloride, urea and water in red blood cells (RBC), and concludes that the urea transporter (UT-B) does not transport water. cms -1 (human). DIDS, DNDS and phloretin inhibit P Cl by >99% in all RBC species. PCMBS, PCMB and phloretin inhibit P urea by >99% in Amphiuma, dog and human RBC, but not in chick and duck RBC. PCMBS and PCMB inhibit P d in duck, dog and human RBC, but not in chick and Amphiuma RBC. Temperature dependence, as measured by apparent activation energy, E A , of P Cl is 117.8 (duck), 74.9 (Amphiuma) and 89.6kJmol −1 (dog). The E A of P urea is 69.6 (duck) and 53.3kJmol −1 (Amphiuma), and that of P d is 34.9 (duck) and 32.1kJmol −1 (Amphiuma). The present and previous RBC studies indicate that anion (AE1), urea (UT-B) and water (AQP1) transporters only transport chloride (all species), water (duck, dog, human) and urea (Amphiuma, dog, human), respectively. Water does not share UT-B with urea, and the solute transport is not coupled under physiological conditions.

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Section: Do Urea and Water Share A Pathway In Common In Rbc?mentioning

confidence: 69%

Section: Do Urea and Water Share A Pathway In Common In Rbc?mentioning

confidence: 98%

The permeability of red blood cells to chloride, urea, and water

Brahm

2013

Journal of Experimental Biology

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“…It was reported that some AQP3 inhibitors suppressed the movement of water through AQP3 expressed in Xenopus oocytes but not the movement of glycerol and urea [19]. Moreover, it has been reported that the transport function of urea transporter 3, another water/cryoprotectant channel, differed depending on the level of its expression in the plasma membrane [20]. When urea transporter 3 was expressed in Xenopus oocytes at a physiological level, it transported only urea, but when it was overexpressed, it transported not only urea but also water and various small neutral solutes.…”

Section: Discussionmentioning

confidence: 99%

Developmental Ability of Vitrified Mouse Oocytes Expressing Water Channels

Yamaji

Seki

Matsukawa

et al. 2011

Journal of Reproduction and Development

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Abstract. Previously, we showed that the exogenous expression of aquaporin 3 (AQP3), an aquaglyceroporin, improved the tolerance of mouse oocytes to vitrification with a glycerol-based solution. In the present study, we examined conditions suitable for the expression of AQP3 and the ability of vitrified oocytes to develop in vitro and in vivo after fertilization. After only partial remove of cumulus cells, immature mouse oocytes (germinal vesicle stage) were injected with 5, 10 or 20 pg of AQP3 cRNA and cultured for 12 h for maturation. When matured oocytes were vitrified with a glycerol-based solution, 57-61% survived regardless of the amount of cRNA injected (5-20 pg). By contrast, no oocytes injected with water (control) survived. When the zona pellucida was removed from the vitrified oocytes and the oocytes were then fertilized in vitro and cultured, the proportions that were fertilized and developed into blastocysts were higher when the amount of cRNA injected was 5 pg than 10-20 pg. When 16 blastocysts were transferred to a pseudopregnant mouse, 5 developed to term, demonstrating that oocytes vitrified after injection of AQP3 cRNA retained the ability to develop to term. The water-permeability of cRNA-injected oocytes was higher than that of control oocytes from the maturing stage to the 1-cell zygote stage, whereas glycerol-permeability was higher only at metaphase II. This indicates that AQP3 was expressed for a relatively short period of time. These results suggest that the transient expression of water/cryoprotectant channels is effective for cryopreserving cells that have low membrane-permeability, such as mammalian oocytes. Key words: Aquaporin, Development, Membrane-permeability, Oocyte, Vitrification (J. Reprod. Dev. 57: [403][404][405][406][407][408] 2011) he permeability of the plasma membrane to water and cryoprotectants is one of the most important factors for successful cryopreservation of oocytes/embryos because it influences the formation of intracellular ice, the toxicity of cryoprotectants and osmotic swelling [1]. For cryopreservation of oocytes/embryos, vitrification has advantages over slow freezing in terms of the simplicity of the method and viability of the cells. As the solution used for vitrification contains a high concentration of cryoprotectants, it is much more toxic than the solution for slow-freezing. Therefore, the permeability of the plasma membrane would affect the survival of cryopreserved cells more in vitrification than in slow freezing. If the permeability is low, insufficient exposure to the cryoprotectants causes formation of intracellular ice. However, excessive exposure results in toxic effects of the cryoprotectants. Therefore, high permeability to water and cryoprotectants would be preferable for vitrification.We showed that a simple one-step method is effective for vitrification of mouse morulae [2] but that a two-step method with a pretreatment with a lower concentration of the cryoprotectant is favorable for vitrifying mouse embryos at early cleavage stages...

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“…Whether urea transporters also transport water has been the subject of considerable interest (10,14,32,39). Early studies by Macey and Farmer (17) suggested that the erythrocyte urea transporter, which we now know to be UT-B, transports water.…”

Section: Discussionmentioning

confidence: 99%

Functional characterization ofActinobacillus pleuropneumoniaeurea transport protein, ApUT

Godara¹,

Smith²,

Bossé³

et al. 2009

American Journal of Physiology-Regulatory, Integrative and Comp

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Urea transporters (UTs) effect rapid flux of urea across biological membranes. In the mammalian kidney, UT activity is essential for effective urine concentration. In bacteria, UT-mediated urea uptake permits intracellular urease to degrade urea to ammonia and CO2, a process that either buffers acid loads or provides nutrient nitrogen. We have characterized the urea transport channel protein ApUT from Actinobacillus pleuropneumoniae. Kinetic analysis of bacterial inside-out membranes enriched in ApUT showed ∼28-fold increase in urea permeability (3.3 ± 0.4 × 10−4cm/s) compared with control vesicles (0.11 ± 0.02 × 10−4cm/s). In addition to urea, ApUT also conducts water. Urea and water transport across the channel was phloretin and mercury inhibitable, and the site of inhibition may be located on the cytoplasmic side of the protein. Glycerol and urea analogs, such as methylamine, dimethylurea, formamide, acetamide, methylurea, propanamide, and ethylamine did not permeate across ApUT.

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At Physiological Expression Levels the Kidd Blood Group/Urea Transporter Protein Is Not a Water Channel

Cited by 67 publications

References 35 publications

The permeability of red blood cells to chloride, urea, and water

The permeability of red blood cells to chloride, urea, and water

Developmental Ability of Vitrified Mouse Oocytes Expressing Water Channels

Functional characterization ofActinobacillus pleuropneumoniaeurea transport protein, ApUT

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