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Human red cell Aquaporin CHIP. II. Expression during normal fetal development and in a novel form of congenital dyserythropoietic anemia
(The American Society for Clinical Investigation, 1994-09)
Channel-forming integral protein (CHIP) is the archetypal member of the Aquaporin family of water channels. Delayed CHIP expression was shown recently in perinatal rat (Smith, B. L., R. Baumgarten, S. Nielsen, D. Raben, ...
Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane: Evidence for a secretin-induced vesicular translocation of aquaporin-1
(American Society for Biochemistry and Molecular Biology, 1997-05-16)
Although secretin is known to stimulate ductal bile secretion by directly interacting with cholangiocytes, the precise cellular mechanisms accounting for this choleretic effect are unknown. We have previously shown that ...
Characterization of aquaporin-6 as a nitrate channel in mammilian cells: Requirement of pore-lining residue threonine 63
(American Society for Biochemistry and Molecular Biology, 2002-10-18)
Aquaporins (AQP) were originally regarded as plasma membrane channels that are freely permeated by water or small uncharged solutes but not by ions. Unlike other aquaporins, AQP6 overexpressed in Xenopus laevis oocytes was ...
Expression of multiple water channel activities in Xenopus oocytes injected with mRNA from rat kidney
(Rockefeller University Press, 1993-06)
To test the hypothesis that renal tissue contains multiple distinct water channels, mRNA prepared from either cortex, medulla, or papilla of rat kidney was injected into Xenopus oocytes. The osmotic water permeability (Pf) ...
Reduced arsenic clearance and increased toxicity in aquaglyceroporin-9-null mice
(National Academy of Sciences, 2009-09-15)
Expressed in liver, aquaglyceroporin-9 (AQP9) is permeated by glycerol, arsenite, and other small, neutral solutes. To evaluate a possible protective role, AQP9-null mice were evaluated for in vivo arsenic toxicity. After ...
Delayed onset of brain edema and mislocalization of aquaporin-4 in dystrophin-null transgenic mice
(National Academy of Sciences, 2002-10-01)
Cerebral water accumulation was studied during induction of brain edema in dystrophin-null transgenic mice (mdx-betageo) and control mice. Immunofluorescence and immunoelectron microscopic analyses of dystrophin-null brains ...
Aquaglyceroporin AQP9: solute permeation and metabolic control of expression in liver
(National Academy of Sciences, 2003-03-04)
Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to glycerol and certain small, uncharged solutes. AQP9 has unusually broad solute permeability and is expressed in hepatocyte plasma ...
Purification and partial characterization of the Mr 30,000 integral membrane protein associated with the erythrocyte Rh(D) antigen
(American Society for Biochemistry and Molecular Biology, 1987-12-25)
Erythrocytes bearing the Rh(D) antigen have an Mr 30,000 integral membrane protein which can be surface-labeled with 125I and can be quantitatively immunoprecipitated from Triton X-100-solubilized spectrin-depleted membrane ...
Molecular struture of the water channel through aquaporin CHIP. The hourglass model.
(American Society for Biochemistry and Molecular Biology, 1994-05-20)
Aquaporin channel-forming integral protein (CHIP) is the first characterized water channel protein (genome symbol AQP1), but the molecular structure of the aqueous pathway through CHIP remains undefined. The two halves of ...
Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord
(National Academy of Sciences, 1998-09-29)
Aquaporin (AQP) water channels are abundant in the brain and spinal cord, where AQP1 and AQP4 are believed to play major roles in water metabolism and osmoregulation. Immunocytochemical analysis of the brain recently ...