Aquaporins by Baoxue Yang (eds.) PDF

By Baoxue Yang (eds.)

ISBN-10: 9402410554

ISBN-13: 9789402410556

ISBN-10: 9402410570

ISBN-13: 9789402410570

This booklet presents a cutting-edge document on our present figuring out of aquaporins and the long run path of the sphere. Aquaporins (AQPs) are a bunch of water-channel proteins which are particularly permeable to water and different small molecules, akin to glycerol and urea. thus far 13 water-channel proteins (AQP0 – AQP12) were cloned and the mechanisms and physiological features of water delivery 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 mobile membranes, and reviews on aquaporin knockout mouse types recommend that aquaporins are concerned with the advance of a few ailments and so they will be precious ambitions of study into selective-inhibitor medicines. via targeting the advances revamped the final twenty years within the biophysics, genetics, protein constitution, molecular biology, body structure, pathophysiology and pharmacology of aquaporins in mammalian cellphone membranes, this ebook presents novel insights into extra mechanisms and the physiological value of water and a few small molecule delivery in mammals which will stimulate additional examine in new directions.

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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.

References 1. Abascal F, Irisarri I, Zardoya R (2014) Diversity and evolution of membrane intrinsic proteins. Agre P, Preston GM, Smith BL, Jung JS, Raina S, Moon C, Guggino WB, Nielsen S (1993) Aquaporin CHIP: the archetypal molecular water channel. Agre P, King LS, Yasui M, Guggino WB, Ottersen OP, Fujiyoshi Y, Engel A, Nielsen S (2002) Aquaporin water channels – from atomic structure to clinical medicine. Almasalmeh A, Krenc D, Wu B, Beitz E (2014) Structural determinants of the hydrogen peroxide permeability of aquaporins.

Ryanodine inhibitors, is physically associated with AQP2 in the princicalmodulin inhibitors, or intracellular Ca2+ chela- pal cells of the kidney collecting ducts [181]. A tors were shown to block vasopressin-stimulated very lately study demonstrated that loss of translocation of AQP2 to the plasma membrane AKAP220 leads to accumulation of AQP2 at the and increase of osmotic water permeability in plasma membrane and reduces urine-diluting primary cultured IMCD cells [35, 38, 257]. These capacity during overhydration [245].

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Aquaporins by Baoxue Yang (eds.)


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