Results 31 to 40 of about 4,789 (161)

Aquaglyceroporin AQP9: Solute permeation and metabolic control of expression in liver [PDF]

open access: yesProceedings of the National Academy of Sciences, 2003
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 membranes.
Agre, Peter   +5 more
openaire   +4 more sources

Defective glycerol metabolism in aquaporin 9 (AQP9) knockout mice [PDF]

open access: yesProceedings of the National Academy of Sciences, 2007
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 remain incomplete and conflicting, we generated AQP9 knockout mice.
Nielsen, S   +7 more
openaire   +2 more sources

Liver glycerol permeability and aquaporin-9 are dysregulated in a murine model of Non-Alcoholic Fatty Liver Disease. [PDF]

open access: yesPLoS ONE, 2013
One form of liver steatosis, namely Non-Alcoholic Fatty Liver Disease (NAFLD), is a worrisome health problem worldwide characterized by intrahepatic triacylglycerol (TG) overaccumulation.
Patrizia Gena   +10 more
doaj   +1 more source

Fluxes of water through aquaporin 9 weaken membrane-cytoskeleton anchorage and promote formation of membrane protrusions. [PDF]

open access: yesPLoS ONE, 2013
All modes of cell migration require rapid rearrangements of cell shape, allowing the cell to navigate within narrow spaces in an extracellular matrix.
Thommie Karlsson   +4 more
doaj   +1 more source

Expression and Localization of Aqua-glyceroporins AQP3 and AQP9 in Rat Oral Epithelia [PDF]

open access: yesThe Bulletin of Tokyo Dental College, 2014
Aquaporins (AQPs) are a family of small integral membrane proteins made up of 6 hydrophobic, a-helical, membrane-spanning domains surrounding a highly selective aqueous pore. AQP3, AQP7, and AQP9, termed aqua-glyceroporins, are known to be involved in the transport of water, glycerol, and other small molecules.
Poveda, M   +6 more
openaire   +3 more sources

Aquaporin 9 in rat brain after severe traumatic brain injury

open access: yesArquivos de Neuro-Psiquiatria, 2012
OBJECTIVE: To reveal the expression and possible roles of aquaporin 9 (AQP9) in rat brain, after severe traumatic brain injury (TBI). METHODS: Brain water content (BWC), tetrazolium chloride staining, Evans blue staining, immunohistochemistry (IHC ...
Hui Liu   +6 more
doaj   +1 more source

Changes in expression of aquaporin-4 and aquaporin-9 in optic nerve after crushing in rats. [PDF]

open access: yesPLoS ONE, 2014
The purpose of this study was to determine the temporal and spatial changes in the expression of AQP4 and AQP9 in the optic nerve after it is crushed. The left optic nerves of rats were either crushed (crushed group) or sham operated (sham group), and ...
Hiroyuki Suzuki   +12 more
doaj   +1 more source

Changes in the Expression of AQP4 and AQP9 in the Hippocampus Following Eclampsia-Like Seizure [PDF]

open access: yesInternational Journal of Molecular Sciences, 2018
Eclampsia is a hypertensive disorder of pregnancy that is defined by the new onset of grand mal seizures on the basis of pre-eclampsia. Until now, the mechanisms underlying eclampsia were poorly understood. Brain edema is considered a leading cause of eclamptic seizures; aquaporins (AQP4 and AQP9), the glial water channel proteins mainly expressed in ...
Han, Xinjia   +5 more
openaire   +2 more sources

Aquaporin 9 (AQP9) Localization in the Adult Dog Testis Excurrent Ducts by Immunohistochemistry [PDF]

open access: yesThe Anatomical Record, 2007
AbstractAquaporins (AQPs) are small, intrinsic membrane proteins that are present in many cell types involved in fluid transport. AQP9 is a major apical water channel that is expressed throughout the efferent ducts, epididymis, and vas deferens, as well as in other regions of the human and rodent male reproductive tract. The target of this study was to
Domeniconi, Raquel Fantin   +4 more
openaire   +3 more sources

Morphophysiological dynamics of the proximal post‐testicular ducts in Crotalus durissus Linnaeus, 1758 (Squamata: Viperidae)

open access: yesThe Anatomical Record, EarlyView.
Abstract The organization and function of reptilian excurrent ducts remain poorly characterized, particularly in Neotropical snakes. We provide the first integrative morphological, histochemical, immunohistochemical, and ultrastructural analysis of the proximal post‐testicular ducts of Crotalus durissus across reproductive stages.
Flávia Cappuccio de Resende   +9 more
wiley   +1 more source

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