1Institutul de Biologie Bucureşti, Academia Română
The priority of Prof. Gheorghe Benga in the discovery of the first water channel protein from the human red blood cell membrane (RBC) membrane a few years before Peter Agre is now acknowledged by the prestigious scientific journal Molecular Aspects of Medicine (Impact Factor ~10), in a special issue of October/December 2012 (volume 33, issues 5-6, pp. 511-703). Benga and coworkers, between 1977 and 1985, extensively assessed the conditions of inhibition of water transport in RBC and resealed ghosts by nuclear magnetic resonance, biochemical methods and electron microscopy, and found several new particular characteristics, for example, the water channels exhibited resistance to proteolysis in intact cells or irreversible inhibition of water transport by fluoresceinmercuric acetate. In 1986, they undoubtedly proved for the first time the presence and location of a water channel protein in the human RBC membrane (after labeling with a specific inhibitor of water diffusion, 203Hg-p-chloromercuribenzene sulfonate: 203Hg-PCMBS) among polypeptides migrating in the region of 35-60 kDa on the electrophoretograms. Benga and coworkers also proposed that a minor membrane protein that binds PCMBS is involved in water transport, and indicated that by purification and reconstitution in liposomes this specific protein could be further characterized.
Water channel proteins, Aquaporins, Human red blood cell membrane
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