By Baoxue Yang (eds.)

ISBN-10: 9402410554

ISBN-13: 9789402410556

ISBN-10: 9402410570

ISBN-13: 9789402410570

This publication presents a cutting-edge record on our present realizing of aquaporins and the long run course of the sphere. Aquaporins (AQPs) are a gaggle of water-channel proteins which are in particular permeable to water and different small molecules, resembling glycerol and urea. to this point 13 water-channel proteins (AQP0 – AQP12) were cloned and the mechanisms and physiological features of water shipping throughout organic membranes have lengthy been the topic of curiosity. contemporary advances within the molecular biology and body structure of water delivery have yielded new insights into how and why water strikes throughout phone membranes, and reports on aquaporin knockout mouse types recommend that aquaporins are excited about the advance of a few illnesses and so they might be precious goals of analysis into selective-inhibitor medicinal drugs. by way of concentrating on the advances revamped the final twenty years within the biophysics, genetics, protein constitution, molecular biology, body structure, pathophysiology and pharmacology of aquaporins in mammalian mobilephone membranes, this ebook presents novel insights into additional mechanisms and the physiological importance of water and a few small molecule delivery in mammals to be able to stimulate extra examine in new directions.

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For the phosphorylation of AQP2, anchoring of PKA by AKAP in close proximity to AQP2 is a prerequisite [51, 177]. Several splice variant of 1 Molecular Biology of Aquaporins AKAP18, AKAP18delta, and AKAP220 has been reported to be involved in the shuttling of AQP2 [83, 117, 118]. 21 the local actin cytoskeleton depolymerization and subsequent exocytosis. 2 The Role of Calcium affinity of AQP2 to myosin-Vb, one of the central in Vasopressin-Induced AQP2 regulators in apical trafficking. This interaction Trafficking results in a reduced quantity of myosin-Vb that Several studies have demonstrated a role of intra- bounds to F-actin, resulting in F-actin destabilicellular Ca2+ mobilization in vasopressin-­ zation that allows translocation of AQP2 vesicles mediated AQP2 trafficking.

Bienert GP, Thorsen M, Schussler MD, Nilsson HR, Wagner A, Tamas MJ, Jahn TP (2008) A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH)3 and Sb(OH)3 across membranes. BMC Biol 6:26 16. Bienert GP, Chaumont F (2014) Aquaporin-­ facilitated transmembrane diffusion of hydrogen peroxide. Bin K, Shi-Peng Z (2011) Acetazolamide inhibits aquaporin-1 expression and colon cancer xenograft tumor growth. Bollag WB, Xie D, Zheng X, Zhong X (2007) A potential role for the phospholipase D2-aquaporin-3 signaling module in early keratinocyte differentiation: production of a phosphatidylglycerol signaling lipid.

Ikeda M, Andoo A, Shimono M, Takamatsu N, Taki A, Muta K, Matsushita W, Uechi T, Matsuzaki T, Kenmochi N, Takata K, Sasaki S, Ito K, Ishibashi K (2011) The NPC motif of aquaporin-11, unlike the NPA motif of known aquaporins, is essential for full expression of molecular function. Inase N, Fushimi K, Ishibashi K, Uchida S, Ichioka M, Sasaki S, Marumo F (1995) Isolation of human aquaporin 3 gene. J Biol Chem 270:17913–17916 97. Inoue T, Nielsen S, Mandon B, Terris J, Kishore BK, Knepper MA (1998) SNAP-23 in rat kidney: colocalization with aquaporin-2 in collecting duct vesicles.

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Aquaporins by Baoxue Yang (eds.)

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