Ribosomal protein L3 mediated the transport of digoxin in Xenopus laevis oocyte

Abstract

Ribosomal protein L3 (RPL3) is known to be an indispensable and essential component for the peptidyltransferase center. In the present study, we found a novel function of RPL3 using a Xenopus laevis oocyte expression system. When expressed in X. oocytes, RPL3 mediated the high affinity transport of [(3)H]digoxin (K(m) = 213.3 ± 46.8 nM) in a time-, concentration-, and sodium-dependent manners. The maximum velocity of the transport of [(3)H]digoxin via RPL3 produced at physiological pH. However, we did not observe RPL3-mediated transport of several organic solutes such as [(14)C]androstenedione, [(3)H]dexamethasone, [(3)H]dehydroepiandrosterone sulfate, [(3)H]L-tryptophan, [(14)C]L-ascorbic acid, [(14)C]α-ketoglutarate, [(14)C]glutarate, [(3)H]methotrexate, [(3)H]bumetanide, [(3)H]probenecid, [(14)C]salicylic acid, [(14)C]theophylline and [(3)H]valproate. Our results suggest that RPL3 functions as a drug carrier protein and may be involved in the digoxin toxicity in the human body.