Aquaporins by Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric

By Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric Beitz (eds.)

The aquaporin box has matured at an incredibly quick velocity and we're on the verge to advance critical concepts to therapeutically modulate aquaporin functionality without delay or through regulatory networks. Key must haves can be found this day: i. a substantial (and turning out to be) variety of aquaporin crystal constructions for the rational layout of inhibitory molecules, ii. tricky molecular dynamics simulation thoughts for theoretical analyses of selectivity mechanisms and docking experiments, iii. complete information on aquaporin immunohistochemistry, iv. aquaporin knockout animals for physiological reviews, and v. assay platforms for compound library screenings. The constitution of this quantity on aquaporins follows the issues laid out above and hence covers the advancements from easy examine to power pharmacological use. located among pharmacology textbooks and up to date clinical papers this ebook offers a well timed assessment for readers from the basic in addition to the utilized disciplines.

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J Am Soc Nephrol 11:376–380 Kamsteeg EJ, Heijnen I, van Os CH, Deen PM (2000) The subcellular localization of an aquaporin2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers. J Cell Biol 151:919–930 Kamsteeg EJ, Hendriks G, Boone M, Konings IB, Oorschot V, van der Sluijs P, Klumperman J, Deen PM (2006) Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel. Proc Natl Acad Sci USA 103:18344–18349 Katsura T, Gustafson CE, Ausiello DA, Brown D (1997) Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells.

Am J Physiol Cell Physiol 289:C1303–C1311 Jahn TP, Møller AL, Zeuthen T, Holm LM, Klaerke DA, Mohsin B, K¨uhlbrandt W, Schjoerring JK (2004) Aquaporin homologues in plants and mammals transport ammonia. FEBS Lett 574: 31–36 Jung JS, Preston GM, Smith BL, Guggino WB, Agre P (1994) Molecular structure of the water channel through aquaporin CHIP: The hourglass model. J Biol Chem 269:14648–14654 Kachadorian WA, Wade JB, DiScala VA (2000) Vasopressin: Induced structural changes in toad bladder luminal membrane.

32 33 36 37 38 38 41 45 45 48 49 50 51 51 Abstract Progress in the structure determination of AQPs has led to a deep understanding of water and solute permeation by these small integral membrane proteins. The atomic structures now available have allowed the water permeation and exclusion of protons to be monitored by molecular dynamics simulations, and have provided a framework for assessing the water and solute permeation in great detail by site-directed mutations.

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