Inhibition of gentamicin uptake into cultured mouse proximal tubule epithelial cells by L-lysine
| Autor: | Jonathan D. Kaunitz, Vierka P. Smith Cummins, Glenn T. Nagami, Delta R. Mishler |
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| Rok vydání: | 1993 |
| Předmět: |
Arginine
Tetrazolium Salts Mice Transgenic Biology Models Biological Epithelium Cell Line Kidney Tubules Proximal Mice medicine Animals Pharmacology (medical) Coloring Agents Antibacterial agent Pharmacology Kidney Lysine Aminoglycoside Apical membrane Molecular biology Culture Media Thiazoles medicine.anatomical_structure Cell culture Toxicity Immunology Gentamicin Gentamicins medicine.drug |
| Zdroj: | Journal of clinical pharmacology. 33(1) |
| ISSN: | 0091-2700 |
| Popis: | Gentamicin uptake and toxicity was studied in a nontransformed cell line obtained from the S1 segment of the proximal tubule epithelium of a transgenic mouse. Cytotoxicity was assayed using the dye 3-(4,-5dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT). Gentamicin uptake was assayed by a fluorescence polarization assay. No differences in toxicity were found among cells incubated for 4 hours in complete culture medium, enriched Kreb's buffer alone, or enriched Krebs' buffer with added 300 micrograms/mL gentamicin, 0.5 mmol/L L-lysine, or gentamicin plus L-lysine. Uptake of 300 micrograms/mL gentamicin was minimal at zero time and increased as a function of time. Uptake of gentamicin at 4 hours was positively correlated with medium gentamicin concentration. Addition of 0.5 mmol/L L-lysine inhibited uptake of 300 micrograms/mL gentamicin 38.9 +/- 10.2%. No other amino acid, including D-lysine or arginine, significantly changed gentamicin uptake. The authors conclude that gentamicin and L-lysine share a specific uptake mechanism located in the apical membrane of renal proximal tubule cells. |
| Databáze: | OpenAIRE |
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