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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 ...
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 ...
Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ
(National Academy of Sciences, 2001-08-14)
Aquaporins are membrane channels selectively permeated by water or water plus glycerol. Conflicting reports have described ion conductance associated with some water channels, raising the question of whether ion conductance ...
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 ...
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 ...
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 ...
Ion Permeation of AQP6 Water Channel Protein: Single-Channel Recordings After Hg2+ Activation
(American Society for Biochemistry and Molecular Biology, 2002-08-09)
Aquaporin-6 (AQP6) has recently been identified as an intracellular vesicle water channel with anion permeability that is activated by low pH or HgCl2. Here we present direct evidence of AQP6 channel gating using patch ...
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 ...
Rapid gating and anion permeability of an intracellular aquaporin
(Nature Publishing Group, 1992-11-11)
Aquaporin (AQP) water-channel proteins are freely permeated by water but not by ions or charged solutes. Although mammalian aquaporins were believed to be located in plasma membranes, rat AQP6 is restricted to intracellular ...