Now showing items 1-10 of 13
Aquaporin water channels: atomic structure molecular dynamics meet clinical medicine
(American Society for Clinical Investigation, 2002-06-01)
Defective Urinary Concentrating Ability Due to a Complete Deficiency of Aquaporin-1
(Massachusetts Medical Society, 2001-07-19)
Aquaporin-1, the archetypal water-channel protein,1 was initially identified in red cells and renal proximal tubular epithelium.2 The gene for aquaporin-1 (AQP1) on chromosome 7 colocalizes with the Colton blood-group ...
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 ...
Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei
(National Academy of Sciences, 2007-02-13)
The malaria parasite can use host plasma glycerol for lipid biosynthesis and membrane biogenesis during the asexual intraerythrocytic development. The molecular basis for glycerol uptake into the parasite is undefined. We ...
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 ...
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 ...
Aquaporins and the respiratory system: advice for a lung investigator
(American Society for Clinical Investigation, 2000-01-01)
Keratinocyte growth factor modulates alveolar epithelial cell phenotype in vitro: expression of aquaporin 5
(American Thoracic Society, 1998-04)
We investigated the role of keratinocyte growth factor (KGF) in regulation of alveolar epithelial cell (AEC) phenotype in vitro. Effects of KGF on cell morphology, expression of surfactant apoproteins A, B, and C (SP-A, ...
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 ...