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Transport ofl-cysteine by rat renal brush border membrane vesicles

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Summary

Brush border membranes were isolated from rat renal cortex by a divalent cation precipitation method.l-35S-cysteine uptake into the vesicles was measured by a rapid filtration method. Only minimal binding of the amino acid to the vesicles was observed. Sodium stimulatesl-cysteine uptake specifically. Anion replacement experiments, experiments in the presence of potassium/valinomycin-induced diffusion potential as well as experiments with a potential-sensitive fluorescent dye document an electrogenic sodium-dependent uptake mechanism forl-cysteine. Tracer replacement experiments as well as the fluorescence experiments indicate a preferential transport ofl-cysteine. Transport ofl-cysteine is inhibited byl-alanine andl-phenylalanine but not byl-glutamic acid and thel-basic amino acids. Initial, linear influx kinetics provide evidence for the existence of two transport sites. The results suggest (a) sodium-dependent mechanism(s) forl-cysteine shared by other neutral amino acids.

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Authors and Affiliations

  1. Department of Physiology, University of Zurich, Rämistraße 69, CH-8028, Zurich, Switzerland

    B. Stieger, G. Stange, J. Biber & H. Murer

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  1. B. Stieger
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  2. G. Stange
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  3. J. Biber
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  4. H. Murer
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Stieger, B., Stange, G., Biber, J. et al. Transport ofl-cysteine by rat renal brush border membrane vesicles. J. Membrain Biol. 73, 25–37 (1983). https://doi.org/10.1007/BF01870338

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  • DOI: https://doi.org/10.1007/BF01870338

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