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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...

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Autores principales: Rambow, Janis, Wu, Binghua, Rönfeldt, Deike, Beitz, Eric
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2014
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.
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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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