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J Biol Chem, Vol. 273, Issue 14, 8407-8412, April 3, 1998
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From the A facilitated diffusion for glycerol is present
in human erythrocytes. Glycerol transporters identified to date belong
to the Major Intrinsic Protein
(MIP) family of integral membrane proteins, and one of them,
aquaporin-3 (AQP3), has been characterized in mammals. Using an
antibody raised against a peptide corresponding to the rat AQP3
carboxyl terminus, we examined the presence of AQP3 in normal and
Colton-null (aquaporin-1 (AQP1)-deficient) human erythrocytes. Three
immunoreactive bands were detected on immunoblots of both normal and
Colton-null red cells, very similar to the bands revealed in rat
kidney, a material in which AQP3 has been extensively studied. By
immunofluorescence, anti-AQP3 antibodies stained the plasma membranes
of both normal and Colton-null erythrocytes. Glycerol transport was
measured on intact erythrocytes by stopped-flow light scattering and on
one-step pink ghosts by a rapid filtration technique. Glycerol
permeability values, similar in both cell types, suggest that AQP1 does
not represent the major path for glycerol movement across red blood
cell membranes. Furthermore, pharmacological studies showed that
Colton-null red cells remain sensitive to water and glycerol flux
inhibitors, supporting the idea that another proteinaceous path,
probably AQP3, mediates most of the glycerol movements across red cell
membranes and represents part of the residual water transport activity
found in AQP1-deficient red cells.
Service de Biologie Cellulaire,
Département de Biologie Cellulaire et Moléculaire,
CEA/Saclay, 91191 Gif-sur-Yvette Cedex, France, and the
§ Institut des Sciences Végétales, CNRS, 91198 Gif-sur-Yvette Cedex, France
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