Now showing items 1-10 of 23
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 ...
Delayed onset of brain edema and mislocalization of aquaporin-4 in dystrophin-null transgenic mice
(National Academy of Sciences, 2002-10-01)
Cerebral water accumulation was studied during induction of brain edema in dystrophin-null transgenic mice (mdx-betageo) and control mice. Immunofluorescence and immunoelectron microscopic analyses of dystrophin-null brains ...
Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord
(National Academy of Sciences, 1998-09-29)
Aquaporin (AQP) water channels are abundant in the brain and spinal cord, where AQP1 and AQP4 are believed to play major roles in water metabolism and osmoregulation. Immunocytochemical analysis of the brain recently ...
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain
(BioMed Central, 2006-05)
BACKGROUND: The aquaporins are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other ...
Genomic organization and developmental expression of aquaporin-5 in lung
(American College of Chest Physicians, 1997-06)
Targeted disruption of the Cl−/HCO3− exchanger Ae2 results in osteopetrosis in mice
(National Academy of Sciences, 2009-02-03)
Osteoclasts are multinucleated bone-resorbing cells responsible for constant remodeling of bone tissue and for maintaining calcium homeostasis. The osteoclast creates an enclosed space, a lacuna, between their ruffled ...
Aquaporin-1 Water Channel Expression in Human Kidney
(American Society for Nephrology, 1997-01)
The pattern of aquaporin-1 water channel protein (AQP1) expression in the human kidney was analyzed by immunocytochemistry using semi-thin and optimized high-resolution immunoelectron microscopy based on freeze-substituted ...
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 ...
Aquaporin-1 water channel protein in lung: ontogeny, steroid-induced expression, and distribution in rat
(American Society for Clinical Investigation, 1996-05-15)
At birth water is rapidly reabsorbed from the distal lung in preparation for alveolar gas exchange. To investigate a potential role for the AQP1 water channel in development, lung membranes from fetal and perinatal rats ...
CHIP28 water channels are localized in constitutively water-permeable segments of the nephron
(Rockefeller University Press, 1993-01)
The sites of water transport along the nephron are well characterized, but the molecular basis of renal water transport remains poorly understood. CHIP28 is a 28-kD integral protein which was proposed to mediate transmembrane ...