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Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution
(National Academy of Sciences, 2005-02-08)
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
Functional requirement of aquaporin-5 in plasma membranes of sweat glands
(National Academy of Sciences, 2002-01-08)
The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3, and AQP5 mRNA were demonstrated in rat paw by reverse transcription (RT)-PCR, but AQP2 and ...
Altered ubiquitination and stability of aquaporin-1 in hypertonic stress
(National Academy of Sciences, 2001-02-27)
Aquaporin-1 (AQP1) water channel protein expression is increased by hypertonic stress. The contribution of changes in protein stability to hypertonic induction of AQP1 have not been described. Incubation of BALB/c fibroblasts ...
Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia
(National Academy of Sciences, 1999-05-01)
All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water transport across cells. Here we show that AQP6 is localized exclusively in intracellular membranes ...
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 ...
Defective glycerol metabolism in aquaporin 9 (AQP9) knockout mice
(National Academy of Sciences, 2007-02-27)
Aquaporin-9 (AQP9) is an aquaglyceroporin membrane channel shown biophysically to conduct water, glycerol, and other small solutes. Because the physiological role/s of AQP9 remain undefined and the expression sites of AQP9 ...
An alpha-syntrophin-dependent pool of AQP4 in astroglial end-feet confers bidirectional water flow between blood and brain
(National Academy of Sciences, 2003-02-18)
The water channel AQP4 is concentrated in perivascular and subpial membrane domains of brain astrocytes. These membranes form the interface between the neuropil and extracerebral liquid spaces. AQP4 is anchored at these ...
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 ...
Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry.
(American Society for Biochemistry and Molecular Biology, 2001-08-24)
The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Here we describe a method to ...