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      Identification of lactate as a driving force for prostanoid transport by prostaglandin transporter PGT.

      American Journal of Physiology - Renal Physiology

      genetics, metabolism, Biological Transport, drug effects, physiology, DNA-Binding Proteins, Deoxyglucose, pharmacology, Dinoprostone, pharmacokinetics, Dose-Response Relationship, Drug, Gene Expression, Glucose, Transfection, Glutamine, Glycolysis, HeLa Cells, Humans, Lactic Acid, Organic Anion Transporters, Oxidative Phosphorylation, Prostaglandins, Antiporters

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          Abstract

          We previously characterized the prostaglandin (PG) transporter PGT as an exchanger in which [(3)H]PGE(2) influx is coupled to the efflux of a countersubstrate. Here, we cultured HeLa cells that stably expressed human PGT under conditions known to favor glycolysis (glucose as a carbon source) or oxidative phosphorylation (glutamine as a carbon source) and studied the effect on PGT-mediated [(3)H]PGE(2) influx. PGT-expressing cells grown in glutamine exhibited a 2- to 4-fold increase in [(3)H]PGE(2) influx compared with the antisense control, whereas cells grown in glucose exhibited a 14-fold increase. In the presence of 10 vs. 25 mM glucose during the uptake, there was a dose-dependent increment in [(3)H]PGE(2) influx. Cis inhibition of [(3)H]PGE(2) influx occurred with lactate at physiological concentrations (apparent K(m) = 48 +/- 12 mM). Preloading with lactate caused a dose-dependent trans stimulation of PGT-mediated [(3)H]PGE(2) uptake, and external lactate caused trans stimulation of PGT-mediated [(3)H]PGE(2) release. Together, these data are consistent with PGT-mediated PG-lactate exchange. Cells engaged in glycolysis would then be poised energetically for prostanoid uptake by means of PGT.

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          Journal
          11997326
          10.1152/ajprenal.00151.2001

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