Cystine and lysine transport in cultured human renal epithelial cells

• Published in: Metabolism, clinical and experimental Vol. 36; no. 4; p. 356
• Main Authors: States, B, Foreman, J, Lee, J, Harris, D, Segal, S
• Format: Journal Article
• Language: English
• Published: United States 01-04-1987
• Subjects: Arginine - metabolism; Binding, Competitive; Biological Transport; Cystine - metabolism; Epithelium - metabolism; Humans; Kidney - cytology; Kidney - metabolism; Kinetics; Lysine - metabolism; Ornithine - metabolism; Sodium - metabolism
• ISSN: 0026-0495
• DOI: 10.1016/0026-0495(87)90207-1

The transport of the amino acids, cystine and lysine, was studied in epithelial cell lines propagated from human kidney cortex. Cystine uptake data were reproducible in different cell lines and did not vary over several cell passages of an individual cell line. The transport of this disulfide amino acid was sodium-dependent with kinetic analysis showing one apparent Kt system of 0.09 mmol/L and Vmax of 0.054 mmol/L cell water/min. Studies of the kinetics of lysine transport, however, revealed two uptake systems with apparent high and low affinities with Kt of 0.14 mmol/L and 5 mmol/L and Vmax of 0.041 and 0.167 mmol/L cell water/min, respectively. Glutamate appeared to be the most potent inhibitor of cystine uptake by these cultured human renal cells and this interaction was competitive. Although cystine did not inhibit lysine uptake, arginine and ornithine were shown to be major inhibitors, thus providing evidence for the presence of a shared dibasic amino acid transport system.