Elliott J L, Saliba K J, Kirk K
School of Biochemistry and Molecular Biology, Faculty of Science, Australian National University, Canberra, A.C.T. 0200, Australia.
Biochem J. 2001 May 1;355(Pt 3):733-9. doi: 10.1042/bj3550733.
The mature, intraerythrocytic form of the human malaria parasite, Plasmodium falciparum, is reliant on glycolysis for its energetic requirements. It produces large quantities of lactic acid, which have to be removed from the parasite's cytosol to maintain the cell's integrity and metabolic viability. Here we show that the monocarboxylates lactate and pyruvate are both transported across the parasite's plasma membrane via a H(+)/monocarboxylate symport process that is saturable and inhibited by the bioflavonoid phloretin. The results provide direct evidence for the presence at the parasite surface of a H(+)-coupled monocarboxylate transporter with features in common with members of the MCT (monocarboxylate transporter) family of higher eukaryotes.
人类疟原虫恶性疟原虫成熟的红细胞内形式，其能量需求依赖糖酵解。它会产生大量乳酸，必须将这些乳酸从寄生虫的胞质溶胶中清除，以维持细胞的完整性和代谢活力。我们在此表明，单羧酸乳酸和丙酮酸都是通过一种H(+)/单羧酸同向转运过程跨寄生虫的质膜运输的，该过程具有饱和性且会被生物类黄酮根皮素抑制。这些结果为寄生虫表面存在一种与高等真核生物的MCT（单羧酸转运蛋白）家族成员具有共同特征的H(+)偶联单羧酸转运蛋白提供了直接证据。
