ArticlePflugers Archiv : European journal of physiology1995
Luminal transport system for H+/organic cations in the rat proximal tubule. Kinetics, dependence on pH; specificity as compared with the contraluminal organic cation-transport system.
Article in Pflugers Archiv : European journal of physiology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Molecular and cellular physiology of organic cation transporter 2.American journal of physiology. Renal physiology · 2019Review
- Correlation between Apparent Substrate Affinity and OCT2 Transport Turnover.The Journal of pharmacology and experimental therapeutics · 2017Article
- Substrate-dependent inhibition of human MATE1 by cationic ionic liquids.The Journal of pharmacology and experimental therapeutics · 2013Article
- Discovery of potent, selective multidrug and toxin extrusion transporter 1 (MATE1, SLC47A1) inhibitors through prescription drug profiling and computational modeling.Journal of medicinal chemistry · 2013Article
- Twelve transmembrane helices form the functional core of mammalian MATE1 (multidrug and toxin extruder 1) protein.The Journal of biological chemistry · 2012Article
- Molecular determinants of ligand selectivity for the human multidrug and toxin extruder proteins MATE1 and MATE2-K.The Journal of pharmacology and experimental therapeutics · 2012Article
- Characterization of MPP+ secretion across human intestinal Caco-2 cell monolayers: role of P-glycoprotein and a novel Na(+)-dependent organic cation transport mechanism.British journal of pharmacology · 2000Article
- Luminal transport system for choline+ in relation to the other organic cation transport systems in the rat proximal tubule. Kinetics, specificity: alkyl/arylamines, alkylamines with OH, O, SH, NH2, ROCO, RSCO and H2PO4-groups, methylaminostyryl, rhodamine, acridine, phenanthrene and cyanine compounds.Pflugers Archiv : European journal of physiology · 1996Article
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Authors and funding
3 authors.
Funding
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Abstract
The efflux of radiolabelled organic cations from the tubular lumen into proximal tubular cells was investigated by using the stop-flow microperfusion method. The efflux rate increased in the sequence: N1-methylnicotinamide (NMeN+) < cimetidine < tetraethylammonium (TEA+) < N-methyl-4-phenylpyridinium (MPP+). Preloading the animals by i.v. infusion or pre perfusion of the peritubular capillaries with NMeN+ increased the efflux rate of MPP+. Luminal efflux was also augmented when the tubular solution was made alkaline with HCO3- or phosphate, whereby HCO3- is more effective than phosphate. Replacement of Na+ by Cs+ showed no effect. With i.v. preloading the animals with NMeN+ and with 25 mM HCO3- in the luminal perfusate the 2-s efflux follows kinetics with a Michaelis constant Km = 0.21 mmol/l and maximal flux Jmax = 0.42 pmol.cm-1.s-1 and a permeability term with P = 37.7 microns2.s-1. Comparing the apparent luminal inhibitory constant values for MPP+ (Kil,MPP+) with the apparent contraluminal Kicl,NMeN+ values of substrates of homologous series, it was found that (1) limitation by molecular size occurs at the contraluminal cell side earlier than at the luminal cell side; (2) affinity increases with hydrophobicity of the substrates at the luminal cell side, with a steeper or equal slope than at the contraluminal cell side; (3) affinity increases with basicity (i.e. pKa values) at the luminal cell side with a steeper slope than at the contraluminal cell side. Taken together, substrates with low hydrophobicity and low basicity interact at the luminal cell side more weakly than at the contraluminal cell side. On the other hand large, hydrophobic substrates have, at the luminal cell side, a higher affinity than at the contraluminal cell side. Many substrates, however, have equal affinity at the luminal and contraluminal cell sides.
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