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Monoclonal antibodies against the renal Na+-D-glucose cotransporter. Identification of antigenic polypeptides and demonstration of functional coupling of different Na+-cotransport systems

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Koepsell,  Hermann
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Korn,  Klaus
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Raszeja-Specht,  Anna
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Bernotat-Danielowski,  Sabine
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Ollig,  Doris
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Koepsell, H., Korn, K., Raszeja-Specht, A., Bernotat-Danielowski, S., & Ollig, D. (1988). Monoclonal antibodies against the renal Na+-D-glucose cotransporter. Identification of antigenic polypeptides and demonstration of functional coupling of different Na+-cotransport systems. The Journal of Biological Chemistry, 263(34), 18419-18429. doi:10.1016/S0021-9258(19)81375-3.


Cite as: http://hdl.handle.net/21.11116/0000-0007-8279-E
Abstract
Eight monoclonal antibodies are described which are directed against the renal Na+-D-glucose cotransporter. In porcine renal brush-border membranes, the antibodies either bind to one or to three polypeptides which have been identified as components of the Na+-D-glucose cotransporter (Neeb, M., Kunz, U., and Koepsell, H., (1987) J. Biol. Chem. 262, 10718-10727). Their molecular weights and isoelectric points are 75,000 and pH 5.5, 60,000 and pH 5.2, and 47,000 and pH 5.4. Six antibodies were able to influence Na+-dependent D-glucose uptake and/or Na+-dependent high affinity phlorizin binding. In the presence of Na+, the binding of all antibodies to native membrane proteins was altered by D-glucose but not by D-mannose. Since this effect was observed with D-glucose concentrations less than 1 x 10(-8) M, a high affinity D-glucose-binding site on the D-glucose transporter has been implied. Some of the antibodies probably interact also with other Na+-coupled transporters since their binding was altered by micromolar concentrations of L-lactate, L-alanine, or L-glutamate but not by the nontransported control substances D-alanine and D-glutamate. L-lactate increased the binding of one antibody in the absence but not in the presence of D-glucose. Effects of L-lactate and L-alanine on the binding of another antibody were only observed when D-glucose was present. Thus, some epitopes on the Na+-D-glucose cotransporter are altered by D-glucose and also by substrates of other Na+ cotransporters. This finding suggests functional coupling of different Na+-cotransport systems.