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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 ...
Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9
(National Academy of Sciences, 2002-04-30)
Much is known about the transport of arsenite and antimonite into microbes, but the identities of mammalian transport proteins are unknown. The Saccharomyces cerevisiae FPS1 gene encodes a membrane protein homologous to ...
Aquaporins in Saccharomyces: Genetic and functional distinctions between laboratory and wild-type strains
(American Society for Biochemistry and Molecular Biology, 1998-10-16)
Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species. The Saccharomyces genome data base contains an open reading frame (here designated AQY1) that encodes a protein ...
Aquaporin 9 is the major pathway for glycerol uptake by mouse erythrocytes, with implications for malarial virulence
(National Academy of Sciences, 2007-07-24)
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 ...
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 ...
Aquaporins in Saccharomyces: Characterization of a second functional water channel protein
(National Academy of Sciences, 2001-01-30)
The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2. Aqy1p has been shown to be a functional aquaporin in some strains, such as Sigma1278b. AQY2 is disrupted by a stop ...
Aquaporin expression and freeze tolerance in Candida albicans
(American Society for Microbiology, 2005-10)
Aquaporins are members of the major intrinsic protein superfamily of integral membrane proteins which enable the transport of water, glycerol, and other solutes across membranes in various organisms. In microorganisms, the ...