Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1
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...
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| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2019-07-01
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| Series: | FEBS Open Bio |
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| Online Access: | https://doi.org/10.1002/2211-5463.12647 |
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| author | Ashok Aspatwar Martti E. E. Tolvanen Hans‐Peter Schneider Holger M. Becker Susanna Narkilahti Seppo Parkkila Joachim W. Deitmer |
| author_facet | Ashok Aspatwar Martti E. E. Tolvanen Hans‐Peter Schneider Holger M. Becker Susanna Narkilahti Seppo Parkkila Joachim W. Deitmer |
| author_sort | Ashok Aspatwar |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-ab381e1e9b8a48028dec0dab185dcb76 |
| institution | OA Journals |
| issn | 2211-5463 |
| language | English |
| publishDate | 2019-07-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj-art-ab381e1e9b8a48028dec0dab185dcb762025-08-20T02:37:29ZengWileyFEBS Open Bio2211-54632019-07-01971204121110.1002/2211-5463.12647Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1Ashok Aspatwar0Martti E. E. Tolvanen1Hans‐Peter Schneider2Holger M. Becker3Susanna Narkilahti4Seppo Parkkila5Joachim W. Deitmer6Faculty of Medicine and Health Technology Tampere University FinlandDepartment of Future Technologies University of Turku FinlandDivision of General Zoology FB Biologie TU Kaiserslautern GermanyDivision of General Zoology FB Biologie TU Kaiserslautern GermanyFaculty of Medicine and Health Technology Tampere University FinlandFaculty of Medicine and Health Technology Tampere University FinlandDivision of General Zoology FB Biologie TU Kaiserslautern GermanyCarbonic 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.https://doi.org/10.1002/2211-5463.12647carbonic anhydrase‐related proteinlactic acidMCT1membrane transporttransporter |
| spellingShingle | Ashok Aspatwar Martti E. E. Tolvanen Hans‐Peter Schneider Holger M. Becker Susanna Narkilahti Seppo Parkkila Joachim W. Deitmer Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1 FEBS Open Bio carbonic anhydrase‐related protein lactic acid MCT1 membrane transport transporter |
| title | Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1 |
| title_full | Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1 |
| title_fullStr | Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1 |
| title_full_unstemmed | Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1 |
| title_short | Catalytically inactive carbonic anhydrase‐related proteins enhance transport of lactate by MCT1 |
| title_sort | catalytically inactive carbonic anhydrase related proteins enhance transport of lactate by mct1 |
| topic | carbonic anhydrase‐related protein lactic acid MCT1 membrane transport transporter |
| url | https://doi.org/10.1002/2211-5463.12647 |
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