TY - JOUR
T1 - Bidirectional water fluxes and specificity for small hydrophilic molecules in aquaporins 0-5.
AU - Meinild, A K
AU - Klærke, Dan Arne
AU - Zeuthen, T
N1 - Keywords: Animals; Aquaporins; Biological Transport; Humans; Mercuric Chloride; Osmosis; Rats; Water; Xenopus laevis
PY - 1998
Y1 - 1998
N2 - The dimensions of the aqueous pore in aquaporins (AQP) 0, 1, 2, 3, 4, and 5 expressed in Xenopus laevisoocytes were probed by comparing the ability of various solutes to generate osmotic flow. By improved techniques, volume flows were determined from initial rates of changes. Identical values for the osmotic water permeability (L p) were obtained in swelling as in shrinkage experiments demonstrating, for the first time, that aquaporins are bidirectional. The reflection coefficients (¿) of urea, glycerol, acetamide, and formamide at 23¿°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 AQP5: 1, 1, 1, 0.8. As seen there is no clear connection between solute size and permeation. At 13¿°C the ¿s for AQP3 were 1, 0.4, 1, and 0.5; functionally, this pore narrows at lower temperatures. HgCl2 reversibly reduced theL p of AQP3 and increased ¿glyc to 1 and ¿form to 0.6. We conclude that the pore of the various aquaporins are structurally different and that a simple steric model is insufficient to explain solute-pore interactions.
AB - The dimensions of the aqueous pore in aquaporins (AQP) 0, 1, 2, 3, 4, and 5 expressed in Xenopus laevisoocytes were probed by comparing the ability of various solutes to generate osmotic flow. By improved techniques, volume flows were determined from initial rates of changes. Identical values for the osmotic water permeability (L p) were obtained in swelling as in shrinkage experiments demonstrating, for the first time, that aquaporins are bidirectional. The reflection coefficients (¿) of urea, glycerol, acetamide, and formamide at 23¿°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 AQP5: 1, 1, 1, 0.8. As seen there is no clear connection between solute size and permeation. At 13¿°C the ¿s for AQP3 were 1, 0.4, 1, and 0.5; functionally, this pore narrows at lower temperatures. HgCl2 reversibly reduced theL p of AQP3 and increased ¿glyc to 1 and ¿form to 0.6. We conclude that the pore of the various aquaporins are structurally different and that a simple steric model is insufficient to explain solute-pore interactions.
U2 - 10.1074/jbc.273.49.32446
DO - 10.1074/jbc.273.49.32446
M3 - Journal article
C2 - 9829975
SN - 0021-9258
VL - 273
SP - 32446
EP - 32451
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 49
ER -