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Am J Physiol Renal Physiol 282: F1097-F1102, 2002; doi:10.1152/ajprenal.00151.2001
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Vol. 282, Issue 6, F1097-F1102, June 2002

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

Brenda S. Chan1, Shinichi Endo2, Naoaki Kanai3, and Victor L. Schuster1

1 Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10461; 2 Department of Urology, Yamanashi Medical University, Yamanashi 409-3898; and 3 Department of BioMedical Engineering, Tokai University, Kanagawa 259-11, Japan

We previously characterized the prostaglandin (PG) transporter PGT as an exchanger in which [3H]PGE2 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 [3H]PGE2 influx. PGT-expressing cells grown in glutamine exhibited a 2- to 4-fold increase in [3H]PGE2 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 [3H]PGE2 influx. Cis inhibition of [3H]PGE2 influx occurred with lactate at physiological concentrations (apparent Km = 48 ± 12 mM). Preloading with lactate caused a dose-dependent trans stimulation of PGT-mediated [3H]PGE2 uptake, and external lactate caused trans stimulation of PGT-mediated [3H]PGE2 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.

biological transport; organic anion transport; glycolysis


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