Stiftung Tierärztliche Hochschule Hannover (TiHo)

Catalytically‐inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT 1

Affiliation
Faculty of Medicine and Health Technology, Tampere University, Finland.
Aspatwar, Ashok;
ORCID
0000-0003-3434-7646
Affiliation
Department of Future Technologies, University of Turku, Finland.
Tolvanen, Martti E. E.;
Affiliation
Division of General Zoology, FB Biologie, TU Kaiserslautern, Germany.
Schneider, Hans-Peter;
GND
13052381X
ORCID
0000-0002-2700-6117
Affiliation
Division of General Zoology, FB Biologie, TU Kaiserslautern, Germany.
Becker, Holger M.;
Affiliation
Faculty of Medicine and Health Technology, Tampere University, Finland.
Narkilahti, Susanna;
ORCID
0000-0001-7323-8536
Affiliation
Faculty of Medicine and Health Technology, Tampere University, Finland.
Parkkila, Seppo;
Affiliation
Division of General Zoology, FB Biologie, TU Kaiserslautern, Germany.
Deitmer, Joachim W.

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.

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