Download Aquaporins by Baoxue Yang (eds.) PDF

By Baoxue Yang (eds.)

This booklet presents a state of the art record on our present knowing of aquaporins and the longer term path of the sector. Aquaporins (AQPs) are a gaggle of water-channel proteins which are particularly permeable to water and different small molecules, reminiscent of glycerol and urea. so far 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. fresh advances within the molecular biology and body structure of water delivery have yielded new insights into how and why water strikes throughout telephone membranes, and reviews on aquaporin knockout mouse versions recommend that aquaporins are considering the advance of a few illnesses and so they will be worthy objectives of study into selective-inhibitor medicinal drugs. by way of concentrating on the advances revamped the final two decades within the biophysics, genetics, protein constitution, molecular biology, body structure, pathophysiology and pharmacology of aquaporins in mammalian telephone membranes, this e-book presents novel insights into additional mechanisms and the physiological value of water and a few small molecule delivery in mammals with the intention to stimulate additional examine in new directions.

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Extra info for Aquaporins

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Nico B, Ribatti D (2010) Aquaporins in tumor growth and angiogenesis. Nielsen S, DiGiovanni SR, Christensen EI, Knepper MA, Harris HW (1993) Cellular and subcellular immunolocalization of vasopressin-regulated water channel in rat kidney. Nielsen S, Chou CL, Marples D, Christensen EI, Kishore BK, Knepper MA (1995) Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci U S A 92:1013–1017 173.

4 Docking and Fusion of Vesicles Bearing AQP2 with the Apical tion of microtubules and actin cytoskeletons are Membrane (Exocytosis) essential in its trafficking. The actin cytoskeleton provides a cage anchoring AQP2 in unstimulated Fusion of AQP2-bearing vesicles with the plasma cells, preventing their exocytosis. The binding of membrane is a key terminal step in vasopressin-­ AVP to V2R causes the depolymerization of regulated water transport. The docking and fusF-actin in collecting duct cells, which is critical ing of AQP2-bearing vesicles is mediated by in promoting the trafficking and fusion of AQP2-­ SNARE (Soluble N-ethylmaleimidesensitive facbearing vesicles with the apical membrane [212, tor attachment protein receptors) mechanisms 259].

Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Preston GM, Jung JS, Guggino WB, Agre P (1993) The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. Procino G, Barbieri C, Tamma G, De Benedictis L, Pessin JE, Svelto M, Valenti G (2008) AQP2 exocytosis in the renal collecting duct – involvement of SNARE isoforms and the regulatory role of Munc18b. Procino G, Barbieri C, Carmosino M, Rizzo F, Valenti G, Svelto M (2010) Lovastatin-induced cholesterol depletion affects both apical sorting and 31 endocytosis of aquaporin-2 in renal cells.

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