title: Aquaporin-1 in the peritoneal membrane: implications for peritoneal dialysis and endothelial cell function.
abstract: PD (peritoneal dialysis) is an established mode of renal replacement therapy, based on the exchange of fluid and solutes between blood in peritoneal capillaries and a dialysate that has been introduced into the peritoneal cavity. The dialysis process involves diffusive and convective transports and osmosis through the PM (peritoneal membrane). Computer simulations predicted that the PM contains ultrasmall pores (radius <3 A, 1 A=10(-10) m), responsible for up to 50% of UF (ultrafiltration), i.e. the osmotically driven water movement during PD. Several lines of evidence suggest that AQP1 (aquaporin-1) is the ultrasmall pore responsible for transcellular water permeability during PD. Treatment with corticosteroids induces the expression of AQP1 in the PM and improves water permeability and UF in rats without affecting the osmotic gradient and permeability for small solutes. Studies in knockout mice provided further evidence that osmotically driven water transport across the PM is mediated by AQP1. AQP1 and eNOS (endothelial nitric oxide synthase) show a distinct regulation within the endothelium lining the peritoneal capillaries. In acute peritonitis, the up-regulation of eNOS and increased release of nitric oxide dissipate the osmotic gradient and prevent UF, whereas AQP1 expression is unchanged. These results illustrate the usefulness of the PM to investigate the role and regulation of AQP1 in the endothelium. The results also emphasize the critical role of AQP1 during PD and suggest that manipulation of AQP1 expression may be used to increase water permeability across the PM.
authors.affiliation: Division of Nephrology, Université catholique de Louvain Medical School, Brussels, Belgium. devuyst@nefr.ucl.ac.be
authors.forename: Olivier
authors.initials: O
authors.lastname: Devuyst
authors.forename: Jie
authors.initials: J
authors.lastname: Ni
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Verbavatz
mesh_terms: D000305:Adrenal Cortex Hormones / Q000378:metabolism; D000818:Animals; D051398:Aquaporin 1; D020346:Aquaporins / Q000378:metabolism* / Q000648:ultrastructure; D001692:Biological Transport / Q000502:physiology; D001789:Blood Group Antigens; D002196:Capillaries / Q000166:cytology; D042783:Endothelial Cells / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D019001:Nitric Oxide Synthase / Q000378:metabolism; D052250:Nitric Oxide Synthase Type III; D010530:Peritoneal Dialysis; D010537:Peritoneum / Q000166:cytology* / Q000378:metabolism*; D010539:Permeability; D014867:Water / Q000378:metabolism
chemical_list: C496020:AQP1 protein, human; D000305:Adrenal Cortex Hormones; D020346:Aquaporins; D001789:Blood Group Antigens; D014867:Water; D051398:Aquaporin 1; C496314:NOS3 protein, human; D019001:Nitric Oxide Synthase; D052250:Nitric Oxide Synthase Type III