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Catalytically inactive carbonic anhydrase-related proteins enhance transport of lactate by MCT1.


ABSTRACT: Carbonic anhydrases (CA) catalyze the reversible hydration of CO2 to protons and bicarbonate and thereby play a fundamental role in the epithelial acid/base transport mechanisms serving fluid secretion and absorption for whole-body acid/base regulation. The three carbonic anhydrase-related proteins (CARPs) VIII, X, and XI, however, are catalytically inactive. Previous work has shown that some CA isoforms noncatalytically enhance lactate transport through various monocarboxylate transporters (MCT). Therefore, we examined whether the catalytically inactive CARPs play a role in lactate transport. Here, we report that CARP VIII, X, and XI enhance transport activity of the MCT MCT1 when coexpressed in Xenopus oocytes, as evidenced by the rate of rise in intracellular H+ concentration detected using ion-sensitive microelectrodes. Based on previous studies, we suggest that CARPs may function as a 'proton antenna' for MCT1, to drive proton-coupled lactate transport across the cell membrane.

SUBMITTER: Aspatwar A 

PROVIDER: S-EPMC6609565 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Catalytically inactive carbonic anhydrase-related proteins enhance transport of lactate by MCT1.

Aspatwar Ashok A   Tolvanen Martti E E MEE   Schneider Hans-Peter HP   Becker Holger M HM   Narkilahti Susanna S   Parkkila Seppo S   Deitmer Joachim W JW  

FEBS open bio 20190611 7


Carbonic anhydrases (CA) catalyze the reversible hydration of CO<sub>2</sub> to protons and bicarbonate and thereby play a fundamental role in the epithelial acid/base transport mechanisms serving fluid secretion and absorption for whole-body acid/base regulation. The three carbonic anhydrase-related proteins (CARPs) VIII, X, and XI, however, are catalytically inactive. Previous work has shown that some CA isoforms noncatalytically enhance lactate transport through various monocarboxylate transp  ...[more]

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2012-03-25 | GSE36625 | GEO