Inhibition of water and solute permeability in human red cells

Macey, Robert L.; Farmer, Robert E.L.

doi:10.1016/0005-2736(70)90130-6

Cited by 349 publications

(181 citation statements)

References 10 publications

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“…showed that cholesterol decreased the nonelectrolyte permeability of unsaturated phosphat idyl choline membranes by primarily effecting the dehydration of the solutes, and concluded, in agreement with Macey and Farmer (1970). that in the red cell membranes, water is the only nonelectrolyte that crosses the membrane substantially through aqueous pores.…”

Section: » Biological Membranes»supporting

confidence: 74%

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

MacGregor¹

1977

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Section: » Biological Membranes»supporting

confidence: 74%

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

MacGregor¹

1977

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“…Erythrocytes are known to be highly permeable to solutes, such as water, urea, and glycerol (16,17). The discovery of aquaporin water channels provided an explanation for the fast water flux across the erythrocyte plasma membrane (2).…”

Section: Discussionmentioning

confidence: 99%

“…Urea transporter B, a urea transporter expressed in erythrocytes and testes, has been shown to be the main route for urea to pass through erythrocyte membranes (18). Glycerol permeability of erythrocytes has long been recognized and can be pharmacologically inhibited by phloretin and mercury (16,19). Nevertheless, the existence of glycerol channels in mouse erythrocytes has been controversial.…”

Section: Discussionmentioning

confidence: 99%

Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence

Liu

Promeneur

Rojek

et al. 2007

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

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Human and rodent erythrocytes are known to be highly permeable to glycerol. Aquaglyceroporin aquaporin (AQP)3 is the major glycerol channel in human and rat erythrocytes. However, AQP3 expression has not been observed in mouse erythrocytes. Here we report the presence of an aquaglyceroporin, AQP9, in mouse erythrocytes. AQP9 levels rise as reticulocytes mature into erythrocytes and as neonatal pups develop into adult mice. Mice bearing targeted disruption of both alleles encoding AQP9 have erythrocytes that appear morphologically normal. Compared with WT cells, erythrocytes from AQP9-null mice are defective in rapid glycerol transport across the cell membrane when measured by osmotic lysis, [ 14 C]glycerol uptake, or stopped-flow light scattering. In contrast, the water and urea permeabilities are intact. Although the physiological role of glycerol in the normal function of erythrocytes is not clear, plasma glycerol is an important substrate for lipid biosynthesis of intraerythrocytic malarial parasites. AQP9-null mice at the age of 4 months infected with Plasmodium berghei survive longer during the initial phase of infection compared with WT mice. We conclude that AQP9 is the major glycerol channel in mouse erythrocytes and suggest that this transport pathway may contribute to the virulence of intraerythrocytic stages of malarial infection.Plasmodium berghei ͉ aquaglyceroporin A quaglyceroporins are transmembrane proteins belonging to the aquaporin (AQP) water channel family (1). Aquaglyceroporins are the only known glycerol channels in mammalian cells. Among 13 identified mammalian aquaporins, AQP3, AQP7, AQP9, and AQP10 represent the aquaglyceroporin subfamily on the basis of their amino acid sequences and solute permeabilities (1). Aquaglyceroporins are also permeable to urea and water when expressed in Xenopus laevis oocytes (1).The first defined water channel, AQP1, was discovered in human erythrocytes (2). The high expression and water permeability of AQP1 in erythrocytes led to the hypothesis that AQP1 is important in adaptation to dramatic osmolarity changes in the circulation (2). In addition to high water permeability, human and rodent erythrocytes are known to be highly permeable to urea and glycerol (3). AQP3 has been identified as the main channel for glycerol transport in human and rat erythrocytes (4). AQP3 has not been detected in mouse erythrocytes, and the glycerol permeability of mouse erythrocytes from AQP3 knockout mice has been shown to not be affected by gene deletion (5). We revisited this question and detected AQP9 expression in mouse erythrocytes. By using AQP9-null mice, we provide evidence that AQP9 is the major pathway for glycerol transport in mouse erythrocytes.The physiological role of aquaglyceroporins in erythrocytes is still not clear. However, recent studies indicate that aquaglyceroporins AQP7 and AQP9 participate in metabolism. Under fasting conditions, up-regulated AQP7 expression in adipocytes facilitates the release of glycerol, which can then be transported through the ...

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“…Because pCMBS inhibits water and urea transport by reacting with sulfhydryl groups of the transporters [26,27], the effect of this reagent on HUT2-mediated urea flux was also examined. Surprisingly, we found no inhibition of urea uptake by 0.5 mM pCMBS (Table 1), although this reagent inhibited the erythroid HUTll-mediated urea flux (74% inhibition).…”

Section: Transport Studiesmentioning

confidence: 99%

Molecular characterization of a new urea transporter in the human kidney

et al. 1996

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A eDNA clone (HUT2) sharing 61.1% and 89.9% sequence identity with the human erythroid (HUTll) and the rabbit (UT2) urea transporters, respectively, was isolated by homology cloning from a human kidney library. HUT2 transcripts were restricted to the kidney and the HUT2 polypeptide was not immunoprecipitated with blood group Kidd-related antibodies (anti-Jk3) in coupled transcriptiontranslation assays. Functional expression studies in Xenopus oocytes demonstrated that HUT2-mediated urea transport was not inhibited by p-chloromercuribenzene sulfonate (pCMBS) which, however, inhibited the urea flux mediated by HUTll. These findings demonstrate that at least two distinct urea transporters are present in human tissues. By in situ hybridization, the gene encoding HUT2 has been assigned to chromosome 18q12.l-q21-1, as found previously for the Kidd/urea transporter HUT11, suggesting that both genes evolved from duplication of a common ancestor.

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Inhibition of water and solute permeability in human red cells

Cited by 349 publications

References 10 publications

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence

Molecular characterization of a new urea transporter in the human kidney

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