Nonenzymatic Augmentation of Lactate Transport via Monocarboxylate Transporter Isoform 4 by Carbonic Anhydrase II

Nonenzymatic Augmentation of Lactate Transport via Monocarboxylate Transporter Isoform 4 by... Monocarboxylate transporters (MCTs) are carriers of high-energy metabolites like lactate and pyruvate, and different MCT isoforms are expressed in a wide range of cells and tissues. Transport activity of MCT isoform 1 (MCT1), heterologously expressed in Xenopus oocytes, has previously been shown to be supported by carbonic anhydrase II (CAII) in a noncatalytic manner. In the present study, we investigated possible interactions of CAII with MCT4, expressed in Xenopus oocytes. MCT4 transport activity is enhanced both by injected and by coexpressed CAII, similar to MCT1, with the highest augmentation at low extracellular pH and low lactate concentrations. CAII-induced augmentation in MCT4 transport activity is independent from the enzyme’s catalytic function, as shown by application of the CA inhibitor ethoxyzolamide and by coexpression of MCT4 with the catalytically inactive mutant CAII-V143Y. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Nonenzymatic Augmentation of Lactate Transport via Monocarboxylate Transporter Isoform 4 by Carbonic Anhydrase II

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Publisher
Springer-Verlag
Copyright
Copyright © 2010 by Springer Science+Business Media, LLC
Subject
Life Sciences; Human Physiology ; Biochemistry, general
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-010-9240-y
Publisher site
See Article on Publisher Site

Abstract

Monocarboxylate transporters (MCTs) are carriers of high-energy metabolites like lactate and pyruvate, and different MCT isoforms are expressed in a wide range of cells and tissues. Transport activity of MCT isoform 1 (MCT1), heterologously expressed in Xenopus oocytes, has previously been shown to be supported by carbonic anhydrase II (CAII) in a noncatalytic manner. In the present study, we investigated possible interactions of CAII with MCT4, expressed in Xenopus oocytes. MCT4 transport activity is enhanced both by injected and by coexpressed CAII, similar to MCT1, with the highest augmentation at low extracellular pH and low lactate concentrations. CAII-induced augmentation in MCT4 transport activity is independent from the enzyme’s catalytic function, as shown by application of the CA inhibitor ethoxyzolamide and by coexpression of MCT4 with the catalytically inactive mutant CAII-V143Y.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Mar 19, 2010

References

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