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Am J Physiol Regul Integr Comp Physiol 278: R1190-R1195, 2000;
0363-6119/00 $5.00
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Vol. 278, Issue 5, R1190-R1195, May 2000

An endogenous monocarboxylate transport in Xenopus laevis oocytes

M. Tosco1, M. N. Orsenigo1, G. Gastaldi2, and A. Faelli1

1 Dipartimento di Fisiologia e Biochimica Generali, Università di Milano, via Celoria 26, I-20133 Milano; and 2 Istituto di Fisiologia Umana, Università di Pavia, via Forlanini 6, I-27100 Pavia, Italy

We investigated the existence of an endogenous system for lactate transport in Xenopus laevis oocytes. 36Cl-uptake studies excluded the involvement of a DIDS-sensitive anion antiporter as a possible pathway for lactate movement. L-[14C]lactate uptake was unaffected by superimposed pH gradients, stimulated by the presence of Na+ in the incubating solution, and severely reduced by the monocarboxylate transporter inhibitor p-chloromercuribenzenesulphonate (pCMBS). Transport exhibited a broad cation specificity and was cis inhibited by other monocarboxylates, mostly by pyruvate. These results suggest that lactate uptake is mediated mainly by a transporter and that the preferred anion is pyruvate. [14C]pyruvate uptake exhibited the same pattern of functional properties evidenced for L-lactate. Kinetic parameters were calculated for both monocarboxylates, and a higher affinity for pyruvate was revealed. Various inhibitors of monocarboxylate transporters reduced significantly pyruvate uptake. These studies demonstrate that Xenopus laevis oocytes possess a monocarboxylate transport system that shares some functional features with the members of the mammalian monocarboxylate cotransporters family, but, in the meanwhile, exhibits some particular properties, mainly concerning cation specificity.

Xenopus oocytes; lactate transport; pyruvate transport


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