Now showing items 1-6 of 6
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 ...
Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein
(National Academy of Sciences, 2001-11-20)
The Aquaporin-4 (AQP4) water channel contributes to brain water homeostasis in perivascular astrocyte endfeet where it is concentrated. We postulated that AQP4 is tethered at this site by binding of the AQP4 C terminus to ...
Decreased pulmonary vascular permeability in aquaporin-1-null humans
(National Academy of Sciences, 2002-01-22)
The molecular determinants of water permeability in the human lung are incompletely defined. Aquaporins (AQP) are water-specific membrane channel proteins. AQP1 is present in endothelial cells in the lung, including those ...
Functional impairment of lens aquaporin in two families with dominantly inherited cataracts
(Oxford University Press, 2000-09-22)
Opacities in the crystalline lens of eye appear with high frequency in the general population. Dominantly inherited cataracts with differing clinical features were found in two families carrying different point mutations ...
Hypertonic induction of aquaporin-5 expression through an ERK-dependent pathway
(American Society for Biochemistry and Molecular Biology, 2000-03-24)
Aquaporin-5 (AQP5) is a water channel protein expressed in lung, salivary gland, and lacrimal gland epithelia. Each of these sites may experience fluctuations in surface liquid osmolarity; however, osmotic regulation of ...
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 ...