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Water movement through lipid bilayers, pores, and plasma membranes : theory and reality

TLDR
In this article, Osmotic equilibria were induced by an Impermeant Solute Tracer Diffusion of Water Single-file Transport (Osmosis) and Gramicidin.
Abstract
THEORY: Osmotic Equilibrium Osmotic Transport (Osmosis) Induced by an Impermeant Solute Tracer Diffusion of Water Single-file Transport Osmotic Transport (Osmosis) LIPID BILAYER MEMBRANES: The Unmodified Membrane Nystatin an Amphotericin B. Gramicidin A PLASMA MEMBRANES: General Considerations The Red Cell Membrane Epithelia: Antidiuretic Hormone (ADH)-Induced Water Permeability Index.

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Low access resistance perforated patch recordings using amphotericin B

TL;DR: These new approaches can provide a substantial increase in versatility and quality for many kinds of electrophysiological measurements and are used to measure single channel currents in a new "outside-out patch" preparation and to measure the resting voltage of epithelial monolayers.
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Structure of a glycerol-conducting channel and the basis for its selectivity.

TL;DR: The crystal structure of the Escherichia coli glycerol facilitator (GlpF) elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded.
Journal ArticleDOI

Cellular and molecular biology of the aquaporin water channels.

TL;DR: The high water permeability characteristic of mammalian red cell membranes is now known to be caused by the protein AQP1, a tetramer with each subunit containing an aqueous pore likened to an hourglass formed by obversely arranged tandem repeats.
Journal ArticleDOI

Aquaporin CHIP: the archetypal molecular water channel

TL;DR: Recognition of CHIP has provided molecular insight into the biological phenomenon of osmotic water movement, and it is hoped that pharmacological modulation ofCHIP function may provide novel treatments of renal failure and other clinical problems.
Journal ArticleDOI

Structure and function of aquaporin water channels

TL;DR: Evidence for possible movement of ions and carbon dioxide through the aquaporins is reviewed here, as well as evidence for direct regulation of aquaporin function by posttranslational modification such as phosphorylation.
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