Molecular Biology and Physiology of Water and Solute Transport [Paperback]

Biophysical studies in the 1950ies and 1960ies led to the realization that the water permeability of certain biological membranes must be due to the presence of water transporting proteins. This hypothesis was confirmed in 1991 and 1992 with the pioneering discovery of the first molecular membrane water channel, CHIP28, by Agre and coworkers. This integral membrane protein, which is abundant in the erythrocyte membrane and in many epithelial cells, is now called aquaporin-1 or AQP1. Thus the terms water channel or aquaporin are synonymous.
In July 2000 more than 200 researchers came together in Gothenburg, Sweden, for the `3rd International Conference on the Molecular Biology and Physiology of Water and Solute Transport to discuss progress in this emerging research field. 58 different presentations from this conference are the basis for this book. Cumulatively, these 58 short chapters provide a balanced overview complementing numerous recent reviews in this field.Structure Function Analysis of Aquaporins and Glycerol Facilitators. Functional Analysis of the Unusual Signature Motifs of the Yeast MIP Channel, Fpslp; R.M. Bill, et al. GLPF: A Structural Variant of the Aquaporin Tetramer; T. Braun, et al. Different Behaviours of MIP Proteins in N-Lauroylsarcosine; L. Duchesne, et al. Overexpression and Purification of the Glycerol Transport Facilitators, Fpslp and GlpF, in Saccharomyces Cerevisiae and Escherichia Coli; K. Hedfalk, et al. Three-Dimensional Fold of Human AQP1 Water Channel Determined by Electron Cryo-Crystallography of 2-Dimensional Crystals Embedded in Ice; A.K. Mitra, et al. Volume Flux Across Red Cell AQP1 and E. Coli AQPZ Water Channel Proteins Reconstituted into Planar Lipid Bilayers; S.M. Saparov, et al. Biogenesis and Folding of Aquaporin Water Channels in the Endoplasmic Reticulum; I. Turnbull, et al. Function, Physiological Roles and Regulation of Mammalian Aquaporins. The Kidney in the Inner Ear; E. Beitló+