期刊
FEBS OPEN BIO
卷 9, 期 7, 页码 1204-1211出版社
WILEY
DOI: 10.1002/2211-5463.12647
关键词
carbonic anhydrase-related protein; lactic acid; MCT1; membrane transport; transporter
资金
- Jane & Aatos Erkko Foundation
- Sigrid Juselius Foundation
- Finnish Funding Agency for Innovation, Tekes
- Academy of Finland
- Finnish Culture Foundation
- Deutsche Forschungsgemeinschaft [DE 231/24-2, BE 4310/6-1]
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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