American Journal of Physiology-Renal Physiology · 1991 · 43 citations · 0 references
Life SciencesBiochemistryPharmacologyBiological Transport PhenomenaIntracellular TransportRenal PathophysiologyIon PermeationMembrane TransportRenal TransportersTransport Across Biological MembranesTransport In CellsActive Renal TransportBrush Border Membrane TransportConcentration Gradient Driven TransportElectrochemical Proton GradientProximal Tubule PhysiologyRenal Transporter FunctionRenal Transporter KineticsTransporter-mediated Renal Elimination
The renal proximal tubule is responsible for the active elimination of organic cations. Studies in brush-border membrane vesicles (BBMV) suggest that active organic cation transport is mediated by an organic cation-proton antiporter. The goals of this study were to determine whether this transporter is expressed in human kidney and to elucidate its characteristics. Transport of the organic cations N1-[3H]methylnicotinamide (NMN) and [14C]tetraethylammonium (TEA) was determined by rapid filtration in BBMV of donor human kidneys. The uptake of NMN and TEA was driven against a concentration gradient by an outwardly directed proton gradient. NMN uptake was inhibited by the organic cations TEA, NMN, quinine, and cimetidine, but was not affected by p-aminohippuric acid, cephalexin, and polyamines. The electroneutral transport of NMN was characterized by a Km of 0.44 +/- 0.07 mM and a Vmax of 24.4 +/- 15.2 pmol.mg protein-1.s-1. The rate of proton efflux from BBMV increased in the presence of an inwardly directed TEA gradient. Preloading BBMV with NMN or TEA trans-stimulated the initial rate of uptake of TEA. Therefore the human proximal tubule expresses an organic cation-proton antiporter in the brush-border membrane. The antiporter is similar to that described in other mammalian species but shows some differences in its transport characteristics.