Journal ArticleDOI
Proteomic knowledge of human aquaporins
Fulvio Magni,Cecilia Sarto,Davide Ticozzi,Monica Soldi,Niccolò Bosso,Paolo Mocarelli,Marzia Galli Kienle +6 more
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TLDR
Proteomic approaches to identify and characterize the most studied AQPs, mainly through SDS‐PAGE followed by MS analysis, are discussed and the clinical importance of the best studied aquaporin (AQP1) in human diseases is provided.Abstract:
Aquaporins (AQPs) are an ubiquitous family of proteins characterized by sequence similarity and the presence of two NPA (Asp-Pro-Ala) motifs. At present, 13 human AQPs are known and they are divided into two subgroups according to their ability to transport only water molecules (AQP0, AQP1, AQP2, AQP4, AQP5, AQP6, and AQP8), or also glycerol and other small solutes (AQP3, AQP7, AQP9, AQP10, AQP12). The genomic, structural, and functional aspects of this family are briefly described. In particular, proteomic approaches to identify and characterize the most studied AQPs, mainly through SDS-PAGE followed by MS analysis, are discussed. Moreover, the clinical importance of the best studied aquaporin (AQP1) in human diseases is also provided.read more
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Human aquaporins : regulators of transcellular water flow
Rebecca E. Day,Philip Kitchen,David Owen,Charlotte E. Bland,Lindsay Marshall,Alex C. Conner,Roslyn M. Bill,Matthew T. Conner +7 more
TL;DR: This review examines the regulatory role of AQPs in transcellular water flow, especially in CVR, and focuses on key systems of the human body, encompassing processes as diverse as urine concentration in the kidney to clearance of brain oedema.
Journal ArticleDOI
Aquaporins with selectivity for unconventional permeants.
B. Wu,Eric Beitz +1 more
TL;DR: This work summarizes the available data on permeability properties and physiological settings of these aquaporins and analyzes which structural features might be connected to permeability for non-water, non-glycerol solutes.
Journal ArticleDOI
circHIPK3 regulates cell proliferation and migration by sponging miR-124 and regulating AQP3 expression in hepatocellular carcinoma
TL;DR: It is shown that miR-124 was downregulated in HCC tissues and that the ectopic expression of mi R-124 inhibited the proliferation and migration of HCC cells and it was proposed that aquaporin 3 (AQP3) is a direct target of miR -124.
Journal ArticleDOI
A look inside: localization patterns and functions of intracellular plant aquaporins.
TL;DR: This review examines the diversity of transport properties and localization patterns of intracellular aquaporins and tries to assess to what extent the diverse aquaporin distribution patterns, in relation to the high degree of compartmentation of plant cells, can be linked to a wide range of cellular functions.
Journal ArticleDOI
Water channel proteins (later called aquaporins) and relatives: Past, present, and future
TL;DR: This is the first review providing in a condensed form an overview of the whole WCP field that became in the last 20 years a very hot area of research in biochemistry and molecular cell biology, with wide and increasing implications.
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Kazuyoshi Murata,Kaoru Mitsuoka,Teruhisa Hirai,Thomas Walz,Peter Agre,J. B. Heymann,Andreas Engel,Yoshinori Fujiyoshi +7 more
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Specialized membrane domains for water transport in glial cells : high-resolution immunogold cytochemistry of aquaporin-4 in rat brain
Søren Nielsen,Erlend A. Nagelhus,Mahmood Amiry-Moghaddam,Charles W. Bourque,Peter Agre,Ole Petter Ottersen +5 more
TL;DR: The highly polarized AQP4 expression indicates that these cells are equipped with specific membrane domains that are specialized for water transport, thereby mediating the flow of water between glial cells and the cavities filled with CSF and the intravascular space.