نتایج جستجو برای: aquaporin 1

تعداد نتایج: 2756237  

Journal: :American journal of physiology. Cell physiology 2007
Chunyi George Huang Todd Lamitina Peter Agre Kevin Strange

Aquaporin channels facilitate the transport of water, glycerol, and other small solutes across cell membranes. The physiological roles of many aquaporins remain unclear. To better understand aquaporin function, we characterized the aquaporin gene family in the nematode Caenorhabditis elegans. Eight canonical aquaporin-encoding genes (aqp) are present in the worm genome. Expression of aqp-2, aqp...

Journal: :The Journal of comparative neurology 2010
Shannon D Shields Katherine D Moore Patricia E Phelps Allan I Basbaum

Olfactory ensheathing glia (OEG) are distinct from other glia in their developmental origin, presence in both the peripheral and central nervous systems, and highly restricted location. OEG are present only in the olfactory lamina propria, olfactory nerve, and the outer two layers of the olfactory bulb, where they envelop bundles of olfactory sensory neuron axons in a manner distinct from myeli...

Journal: :The Journal of biological chemistry 2004
Satoshi P Tsunoda Burkhard Wiesner Dorothea Lorenz Walter Rosenthal Peter Pohl

Aquaporin-1 (AQP1) is a membrane channel that allows rapid water movement driven by a transmembrane osmotic gradient. It was claimed to have a secondary function as a cyclic nucleotide-gated ion channel. However, upon reconstitution into planar bilayers, the ion channel exhibited a 10-fold lower single channel conductance than in Xenopus oocytes and a 100-fold lower open probability (<10(-6)) o...

Journal: :Journal of cell science 2005
Samira Saadoun Marios C Papadopoulos Hiroyuki Watanabe Donghong Yan Geoffrey T Manley A S Verkman

Aquaporin-4, the major water-selective channel in astroglia throughout the central nervous system, facilitates water movement into and out of the brain. Here, we identify a novel role for aquaporin-4 in astroglial cell migration, as occurs during glial scar formation. Astroglia cultured from the neocortex of aquaporin-4-null mice had similar morphology, proliferation and adhesion, but markedly ...

Journal: :The Journal of experimental biology 2006
Christian Müller Matthias Sendler Jan-Peter Hildebrandt

Using primers against highly conserved regions of mammalian and bird aquaporins in RT-PCR experiments, we amplified products derived from duck (Anas platyrhynchos) nasal gland RNA that were identified as homologues of mammalian and chicken aquaporin 1 and aquaporin 5 cDNAs by sequencing. Using digoxigenin-labelled probes derived from these PCR products in northern blot analyses of mRNA isolated...

Journal: :The Journal of Cell Biology 2001
Marvin E. Adams Heather A. Mueller Stanley C. Froehner

alpha-Syntrophin is a scaffolding adapter protein expressed primarily on the sarcolemma of skeletal muscle. The COOH-terminal half of alpha-syntrophin binds to dystrophin and related proteins, leaving the PSD-95, discs-large, ZO-1 (PDZ) domain free to recruit other proteins to the dystrophin complex. We investigated the function of the PDZ domain of alpha-syntrophin in vivo by generating transg...

Journal: :Investigative ophthalmology & visual science 2008
Ianors Iandiev Antje Wurm Margrit Hollborn Peter Wiedemann Christian Grimm Charlotte E Remé Andreas Reichenbach Thomas Pannicke Andreas Bringmann

PURPOSE In addition to photoreceptor degeneration, excessive light causes degenerative alterations in the inner retina and ganglion cell death. A disturbance in osmohomeostasis may be one causative factor for the alterations in the inner retina. Because Müller cells mediate inner retinal osmohomeostasis (mainly through channel-mediated transport of potassium ions and water), the authors investi...

Journal: :Kobunshi 2002

Journal: :Genes to Cells 2021

Aquaporin-4 is a transmembrane water channel protein, the C-terminal domain of which facing cytosol. In process investigating role aquaporin-4 with regard to intracellular trafficking, we observed that derivative aquaporin-4, in 53 amino acids had been removed (?271-323), was localized compartments, including endoplasmic reticulum, but not expressed on plasma membranes. This determined by immun...

Journal: :Annals of the New York Academy of Sciences 2005
Anne-Sophie Martinez Gillian Wilson Claire Phillips Christopher Cutler Neil Hazon Gordon Cramb

Long-term cortisol infusion into freshwater (FW)-adapted eels induced a significant increase in aquaporin-1 (AQP1) mRNA expression within the esophageal epithelium of migratory "silver" eels, but not in nonmigratory, immature "yellow" eels. Cortisol treatment had no significant effect on the mRNA abundance of a second aquaporin-1 isoform, termed AQP1dup, which exhibited a highly variable expres...

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