By Stefan Hohmann
Aquaporins summarizes the current wisdom during this increasing box of study, beginning with the structural research of water channel proteins. next chapters commence with mammalian aquaporins, studying body structure and pathophysiology, research of knock-out version animals, and the rules of aquaporin functionality. additionally coated is the distribution and law of aquaporins in crops and the functionality of water and glycerol channels in microbial structures. Key positive factors* entire remedy of a topical examine box* Authored by way of global leaders within the box* Covers structural biology and body structure* Covers diverse experimental and organic structures* Chapters on plant and microbial platforms* vast therapy of mammalian body structure and pathophysiology* Structural research excellently illustrated
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J. Biol. Chem. 269, 21845–21849. , Kuo, W. , and Verkman, A. S. (1995). cDNA cloning and gene structure of a novel water channel expressed exclusively in human kidney: Evidence for a gene cluster of aquaporins at chromosome locus 12q13. Genomics 35, 543–550. , Carlson, E. , Epstein, C. , and Verkman, A. S. (1999). Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. J. Biol. Chem. 274, 20071–20074. Macey, R. I. (1984). Transport of water and urea in red blood cells.
III. OTHER MAMMALIAN AQUAPORINS Discovery of AQP1 rapidly led to homology cloning efforts in multiple laboratories. Curiously, each new homolog was simultaneously reported by different research groups. This mini-industry has identified 10 mammalian homologs, and several have been partially characterized (Fig. 8). A. Orthodox Aquaporins The first characterized member of the family, AQP1, is freely permeated by water but not by other solutes. Several other members of the family were also found to be highly water selective.
Maurel, C. (1997). Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mol. Biol. 48, 399–429. , Schroeder, J. , and Chrispeels, M. J. (1993). The vacuolar membrane protein gamma-TIP creates water specific channels in Xenopus oocytes. EMBO J. 12, 2241–2247. , Schroeder, J. , Chrispeels, M. , and Saier, M. H. J. (1994). Functional characterization of the Escherichia coli glycerol facilitator, GlpF, in Xenopus oocytes. J. Biol. Chem. 269, 11869–11872. , and Fujiyoshi, Y.