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Please use this identifier to cite or link to this item: http://hdl.handle.net/10451/3901

Title: Lack of Aquaporin 3 in bovine erythrocyte membranes correlates with low glycerol permeation
Authors: Campos, Elisa
Moura, Teresa F.
Oliva, Abel
Leandro, Paula
Soveral, Graça
Keywords: Aquaporin 3
Glycerol permeability
Water transport
Erythrocyte
Bovine
Issue Date: 2011
Publisher: Elsevier
Citation: Biochemical and Biophysical Research Communications. May 2011; 408 (3): 477-481
Abstract: In general, erythrocytes are highly permeable to water, urea and glycerol. However, expression of aquaporin isoforms in erythrocytes appears to be species characteristic. In the present study, human (hRBC) and bovine (bRBC) erythrocytes were chosen for comparative studies due to their significant difference in membrane glycerol permeability. Osmotic water permeability (Pf) at 23 ºC was (2.89 ± 0.37) × 10-2 and (5.12 ± 0.61) × 10-2 cm s-1 for human and bovine cells respectively, with similar activation energies for water transport. Glycerol permeability (Pgly) for human ((1.37 ± 0.26) × 10-5 cm s-1) differed in three orders of magnitude from bovine erythrocytes ((5.82 ± 0.37) ×10-8 cm s-1) that also showed higher activation energy for glycerol transport. When compared to human, bovine erythrocytes showed a similar expression pattern of AQP1 glycosylated forms on immunoblot analysis, though in slight higher levels, which could be correlated with the 1.5-fold larger Pf found. However, AQP3 expression was not detectable. Immunofluorescence analysis confirmed the absence of AQP3 expression in bovine erythrocyte membranes. In conclusion, lack of AQP3 in bovine erythrocytes points to the lipid pathway as responsible for glycerol permeation and explains the low glycerol permeability and high Ea for transport observed in ruminants.
Description: NOTICE: this is the author’s version of a work that was accepted for publication in Biochemical and Biophysical Research Communications. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Biochemical and Biophysical Research Communications. May 2011; 408 (3): 477-481.
Peer Reviewed: yes
URI: http://dx.doi.org/10.1016/j.bbrc.2011.04.057
http://hdl.handle.net/10451/3901
ISSN: 0006-291X
Publisher version: http://www.sciencedirect.com/science/article/pii/S0006291X11006425
Appears in Collections:FF-DBBH - Artigos em Revistas Internacionais

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