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NDT Advance Access originally published online on April 20, 2006
Nephrology Dialysis Transplantation 2006 21(8):2069-2071; doi:10.1093/ndt/gfl162
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© The Author [2006]. Published by Oxford University Press on behalf of ERA-EDTA. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Translational Nephrology

Aquaporin-1—a water channel on the move*

Hendrica Belge and Olivier Devuyst

Division of Nephrology, Université catholique de Louvain Medical School, B-1200 Brussels, Belgium

Correspondence and offprint requests to: Olivier Devuyst, MD, PhD, Service de Néphrologie, Université catholique de Louvain, Avenue Hippocrate 10, B-1200 Bruxelles, Belgique. Email: devuyst@nefr.ucl.ac.be

Keywords: cell migration; endothelium; proximal tubule; angiogenesis; wound healing; water transport

The first 10% of the full text of this article appears below.



   Aquaporin-1, a water channel involved in urinary concentrating ability
 
The aquaporins (AQPs) constitute a family of transmembrane, channel-forming glycoproteins, which provide a molecular pathway for the rapid transport of water across biological membranes. These proteins are conserved in bacteria, plants and mammals [1]. The first AQP was identified in 1988 by Peter Agre and his colleagues [2], who were at the time investigating the Rhesus blood group antigens. Using antibodies raised against proteins from the membranes of red blood cells, they purified a peculiar protein that was located in the proximal tubules and descending thin limbs of Henle's loop, i.e. in the exact nephron segments harbouring a constitutive water permeability [2]. After cloning the cDNA and analysing the predicted 269 amino acid polypeptide, they called the newly identified protein . . . [Full Text of this Article]



   From water handling to angiogenesis and cell migration
 


   How aquaporins could participate in cell migration
 


   Conclusions
 

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W. Zhang, E. Zitron, M. Homme, L. Kihm, C. Morath, D. Scherer, S. Hegge, D. Thomas, C. P. Schmitt, M. Zeier, et al.
Aquaporin-1 Channel Function Is Positively Regulated by Protein Kinase C
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[Abstract] [Full Text] [PDF]