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Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions
Classically, aquaporins are divided based on pore selectivity into water specific, orthodox aquaporins and solute-facilitating aquaglyceroporins, which conduct, e.g., glycerol and urea. However, more aquaporin-passing substrates have been identified over the years, such as the gasses ammonia and car...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150397/ https://www.ncbi.nlm.nih.gov/pubmed/25225485 http://dx.doi.org/10.3389/fphar.2014.00199 |
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author | Rambow, Janis Wu, Binghua Rönfeldt, Deike Beitz, Eric |
author_facet | Rambow, Janis Wu, Binghua Rönfeldt, Deike Beitz, Eric |
author_sort | Rambow, Janis |
collection | PubMed |
description | Classically, aquaporins are divided based on pore selectivity into water specific, orthodox aquaporins and solute-facilitating aquaglyceroporins, which conduct, e.g., glycerol and urea. However, more aquaporin-passing substrates have been identified over the years, such as the gasses ammonia and carbon dioxide or the water-related hydrogen peroxide. It became apparent that not all aquaporins clearly fit into one of only two subfamilies. Furthermore, certain aquaporins from both major subfamilies have been reported to conduct inorganic anions, such as chloride, or monoacids/monocarboxylates, such as lactic acid/lactate. Here, we summarize the findings on aquaporin anion transport, analyze the pore layout of such aquaporins in comparison to prototypical non-selective anion channels, monocarboxylate transporters, and formate–nitrite transporters. Finally, we discuss in which scenarios anion conducting aquaporins may be of physiological relevance. |
format | Online Article Text |
id | pubmed-4150397 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-41503972014-09-15 Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions Rambow, Janis Wu, Binghua Rönfeldt, Deike Beitz, Eric Front Pharmacol Pharmacology Classically, aquaporins are divided based on pore selectivity into water specific, orthodox aquaporins and solute-facilitating aquaglyceroporins, which conduct, e.g., glycerol and urea. However, more aquaporin-passing substrates have been identified over the years, such as the gasses ammonia and carbon dioxide or the water-related hydrogen peroxide. It became apparent that not all aquaporins clearly fit into one of only two subfamilies. Furthermore, certain aquaporins from both major subfamilies have been reported to conduct inorganic anions, such as chloride, or monoacids/monocarboxylates, such as lactic acid/lactate. Here, we summarize the findings on aquaporin anion transport, analyze the pore layout of such aquaporins in comparison to prototypical non-selective anion channels, monocarboxylate transporters, and formate–nitrite transporters. Finally, we discuss in which scenarios anion conducting aquaporins may be of physiological relevance. Frontiers Media S.A. 2014-09-01 /pmc/articles/PMC4150397/ /pubmed/25225485 http://dx.doi.org/10.3389/fphar.2014.00199 Text en Copyright © 2014 Rambow, Wu, Rönfeldt and Beitz. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Pharmacology Rambow, Janis Wu, Binghua Rönfeldt, Deike Beitz, Eric Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
title | Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
title_full | Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
title_fullStr | Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
title_full_unstemmed | Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
title_short | Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
title_sort | aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen–host interactions |
topic | Pharmacology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150397/ https://www.ncbi.nlm.nih.gov/pubmed/25225485 http://dx.doi.org/10.3389/fphar.2014.00199 |
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