Bidirectional water fluxes and specificity for small hydrophilic moleculesin aquaporins 0-5

Citation
Ak. Meinild et al., Bidirectional water fluxes and specificity for small hydrophilic moleculesin aquaporins 0-5, J BIOL CHEM, 273(49), 1998, pp. 32446-32451
Citations number
41
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
273
Issue
49
Year of publication
1998
Pages
32446 - 32451
Database
ISI
SICI code
0021-9258(199812)273:49<32446:BWFASF>2.0.ZU;2-9
Abstract
The dimensions of the aqueous pore in aquaporins (AQP) 0, 1, 2, 3, 4, and 5 expressed in Xenopus laevis oocytes were probed by comparing the ability o f various solutes to generate osmotic flow. By improved techniques, volume flows were determined from initial rates of changes. Identical values for t he osmotic water permeability (L-p) were obtained in swelling as in shrinka ge experiments demonstrating, for the first time, that aquaporins are bidir ectional. The reflection coefficients (sigma) of urea, glycerol, acetamide, and formamide at 23 degrees C were: AQP0: 1, 1, 0.8, 0.6; AQP1: 1, 0.8, 1, 1; AQP2: 1, 0.8, 1, 1; AQP3: 1, 0.2, 0.7, 0.4; AQP4: 1, 0.9, 1, 1; and AQP 5: 1, 1, 1, 0.8. As seen there is no clear connection between solute size a nd permeation. At 13 degrees C the sigma s for AQP3 were 1, 0.4, 1, and 0.5 ; functionally, this pore narrows at lower temperatures. HgCl2 reversibly r educed the L-p of AQP3 and increased sigma(glyc) to 1 and sigma(form) to 0. 6. We conclude that the pore of the various aquaporins are structurally dif ferent and that a simple steric model is insufficient to explain solute-por e interactions.