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Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium
The goal of this study was to test for expression of HCO(3)(−) exchangers SLC26A3 and SLC26A6 in primary cultures of porcine vas deferens epithelial cells (1°PVD) and native porcine vas deferens. Quantitative RT-PCR revealed that mRNA coding for SLC26A6 was six times more abundant than mRNA coding f...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BlackWell Publishing Ltd
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4425982/ https://www.ncbi.nlm.nih.gov/pubmed/25907791 http://dx.doi.org/10.14814/phy2.12380 |
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author | Pierucci-Alves, Fernando Akoyev, Vladimir Schultz, Bruce D |
author_facet | Pierucci-Alves, Fernando Akoyev, Vladimir Schultz, Bruce D |
author_sort | Pierucci-Alves, Fernando |
collection | PubMed |
description | The goal of this study was to test for expression of HCO(3)(−) exchangers SLC26A3 and SLC26A6 in primary cultures of porcine vas deferens epithelial cells (1°PVD) and native porcine vas deferens. Quantitative RT-PCR revealed that mRNA coding for SLC26A6 was six times more abundant than mRNA coding for SLC26A3 in 1°PVD cells. Western blot analyses combined with surface biotinylation of 1°PVD demonstrated SLC26A3 and SLC26A6 immunoreactivities in whole-cell lysates and apical surfaces of monolayers. Laser scanning confocal microscopy (LSCM) of the 1°PVD cell monolayers demonstrated that SLC26A3 immunoreactivity was primarily in the apical region but present throughout the basal-apical cellular axis, whereas SLC26A6 immunoreactivity was present in the apical region and sometimes accumulated in the nuclear region. LSCM also demonstrated SLC26A3 and SLC26A6 immunoreactivities present along the entire apical lining of the native porcine vas deferens epithelium and in basal cells. The patterns and apparent abundance of SLC26A3 and SLC26A6 immunoreactivities in the proximal vas deferens were not different from the corresponding immunoreactivities in the distal region. There is no evidence of preferential expression of SLC26A3 or SLC26A6 in any portion of the vas deferens, as has been proposed for epithelia that secrete HCO(3)(−) in other duct systems. Thus, vas deferens epithelia express transporters throughout the duct that can contribute to rapid alkalinization of the luminal contents as it has been demonstrated in vivo. |
format | Online Article Text |
id | pubmed-4425982 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BlackWell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-44259822015-05-14 Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium Pierucci-Alves, Fernando Akoyev, Vladimir Schultz, Bruce D Physiol Rep Original Research The goal of this study was to test for expression of HCO(3)(−) exchangers SLC26A3 and SLC26A6 in primary cultures of porcine vas deferens epithelial cells (1°PVD) and native porcine vas deferens. Quantitative RT-PCR revealed that mRNA coding for SLC26A6 was six times more abundant than mRNA coding for SLC26A3 in 1°PVD cells. Western blot analyses combined with surface biotinylation of 1°PVD demonstrated SLC26A3 and SLC26A6 immunoreactivities in whole-cell lysates and apical surfaces of monolayers. Laser scanning confocal microscopy (LSCM) of the 1°PVD cell monolayers demonstrated that SLC26A3 immunoreactivity was primarily in the apical region but present throughout the basal-apical cellular axis, whereas SLC26A6 immunoreactivity was present in the apical region and sometimes accumulated in the nuclear region. LSCM also demonstrated SLC26A3 and SLC26A6 immunoreactivities present along the entire apical lining of the native porcine vas deferens epithelium and in basal cells. The patterns and apparent abundance of SLC26A3 and SLC26A6 immunoreactivities in the proximal vas deferens were not different from the corresponding immunoreactivities in the distal region. There is no evidence of preferential expression of SLC26A3 or SLC26A6 in any portion of the vas deferens, as has been proposed for epithelia that secrete HCO(3)(−) in other duct systems. Thus, vas deferens epithelia express transporters throughout the duct that can contribute to rapid alkalinization of the luminal contents as it has been demonstrated in vivo. BlackWell Publishing Ltd 2015-04-23 /pmc/articles/PMC4425982/ /pubmed/25907791 http://dx.doi.org/10.14814/phy2.12380 Text en © 2015 The Authors. Physiological Reports published by Wiley Periodicals, Inc. on behalf of the American Physiological Society and The Physiological Society. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Research Pierucci-Alves, Fernando Akoyev, Vladimir Schultz, Bruce D Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium |
title | Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium |
title_full | Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium |
title_fullStr | Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium |
title_full_unstemmed | Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium |
title_short | Bicarbonate exchangers SLC26A3 and SLC26A6 are localized at the apical membrane of porcine vas deferens epithelium |
title_sort | bicarbonate exchangers slc26a3 and slc26a6 are localized at the apical membrane of porcine vas deferens epithelium |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4425982/ https://www.ncbi.nlm.nih.gov/pubmed/25907791 http://dx.doi.org/10.14814/phy2.12380 |
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