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Cell Biology International (2003) 27, 701–709 (Printed in Great Britain)

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Birth of water channel proteins—the aquaporins

Gheorghe Benga*

Department of Cell and Molecular Biology, “Iuliu Haţieganu” University of Medicine and Pharmacy, 6 Pasteur St, 3400,Cluj-Napoca, Romania

Abstract

If we compare aquaporin (as a proteic pathway for water permeation across biological membranes) with a child we can say that he had a very long gestation period. His possible existence was predicted for a long time (Overton in 1985, Stein and Danielli in 1956), some of his features (transport of water and its reversible inhibition) were assigned by Macey and Farmer in 1970, however this child was first detected by Benga and coworkers in 1986. We clearly demonstrated for the first time the presence and location of a water channel at the human RBC membrane among the polypeptides migrating in the region having 35–60 kDa on the electrophoretogram of RBC membranes, labeled with 203Hg-PCMBS in the conditions of specific inhibition of water diffusion; I suggested that a minor membrane protein that binds PCMBS is involved in water transport and also indicated the way in which the specific protein could be further characterized: by purification and reconstitution in liposomes. Our landmark papers in 1986 can be compared with the first detection of a child “in utero” by ultrasonography, since we discovered one of the essential components of the “aquaporin child” (a molecular weight of 35–60 kDa for the glycosylated component); we have also indicated the way to recognize him after birth (among other children of his group!): placing the isolated children in a certain environment and asking them to perform the same task (one should read: reconstitution studies in liposomes and measurement of water permeability), like aligning athletes for a running test. This was the only certain way to know that the child is really the fastest runner and not just one that is helping (by various means) another child to be fastest runner. A “new child” was observed in 1988 by Agre and coworkers, who identified a novel integral membrane protein in human RBCs having a non-glycosylated component of 28 kDa and a glycosylated component migrating as a diffuse band of 35–60 kDa; they suggested that the new protein (nick-named CHIP28 in 1991) may play a role in linkage of the membrane skeleton to the lipid bilayer. In 1992 Agre and coworkers suggested that CHIP28 is a functional unit of membrane water channels; by reconstitution in liposomes it was demonstrated that CHIP28 is a water channel itself rather than a water channel regulator. In other words the child we first detected was recognized as having the predicted qualities only in 1992. In 1993 CHIP28 was renamed aquaporin 1. Looking in retrospect, asking the crucial question, when was the first water channel protein, aquaporin 1, discovered, a fair and clear cut answer would be: the first water channel protein, now called aquaporin 1, was identified or “seen” in situ in the human RBC membrane by Benga and coworkers in 1986. It was again “seen” when it was by chance purified by Agre and coworkers in 1988 and was again identified when its main feature, the water transport property was found by Agre and coworkers in 1992. If a comparison with the discovery of The New World of America is made, the first man who has “seen” a part, very small indeed, of The New Land was Columbus; later, others, including Amerigo Vespucci (from whom the name derived), have better “seen” a larger part of the new Continent and in the subsequent years many explorers discovered the complexity of the Americas!

Key words: Water permeability, Water channel proteins, Aquaporin, Red blood cells.

^*Corresponding author. Tel.: +40-264-594373; fax: +40-264-597257

Received 7 April 2003/24 April 2003; accepted 14 July 2003