Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence
- 24 July 2007
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 104 (30), 12560-12564
- https://doi.org/10.1073/pnas.0705313104
Abstract
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.Keywords
This publication has 29 references indexed in Scilit:
- Defective glycerol metabolism in aquaporin 9 (AQP9) knockout miceProceedings of the National Academy of Sciences of the United States of America, 2007
- Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium bergheiProceedings of the National Academy of Sciences of the United States of America, 2007
- Erythroid Expression and Oligomeric State of the AQP3 ProteinPublished by Elsevier BV ,2002
- Evidence for the Presence of Aquaporin-3 in Human Red Blood CellsPublished by Elsevier BV ,1998
- Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens.JCI Insight, 1994
- Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 ProteinScience, 1992
- Acidified Glycerol Lysis Test: a Screening Test for SpherocytosisBritish Journal of Haematology, 1980
- Some aspects of the osmotic lysis of erythrocytes III. Comparison of glycerol permeability and lipid composition of red blood cell membranes from eight mammalian speciesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- Inhibition of water and solute permeability in human red cellsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1970
- Passage of Glucose and Glycerol across the Red Cell MembraneNature, 1954