Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts
Aquaporins may facilitate transepithelial water absorption in the intestine of seawater (SW)-acclimated fish. Here we have characterized three full-length aqp8 paralogs from Atlantic salmon (Salmo salar). Bayesian inference revealed that each paralog is a representative of the three major classes of...
Published in: | Journal of Experimental Biology |
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Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
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2013
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Online Access: | https://portal.findresearcher.sdu.dk/da/publications/19513a81-36e3-4822-8ef2-a65abc627277 https://doi.org/10.1242/jeb.087890 |
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ftsydanskunivpub:oai:sdu.dk:publications/19513a81-36e3-4822-8ef2-a65abc627277 2024-05-19T07:37:37+00:00 Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts Engelund, Morten Buch Chauvigné, François Christensen, Birgitte M Finn, Roderick N Cerdà, Joan Madsen, Steffen S 2013 https://portal.findresearcher.sdu.dk/da/publications/19513a81-36e3-4822-8ef2-a65abc627277 https://doi.org/10.1242/jeb.087890 eng eng https://portal.findresearcher.sdu.dk/da/publications/19513a81-36e3-4822-8ef2-a65abc627277 info:eu-repo/semantics/restrictedAccess Engelund , M B , Chauvigné , F , Christensen , B M , Finn , R N , Cerdà , J & Madsen , S S 2013 , ' Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts ' , Journal of Experimental Biology , vol. 216 , no. 20 , pp. 3873-3885 . https://doi.org/10.1242/jeb.087890 Aquaporin Evolution Intestine Neofunctionalization Osmoregulation Salmon Salmo salar/metabolism Cell Membrane Permeability Molecular Sequence Data Gene Expression Profiling Phylogeny RNA Messenger/genetics Time Factors Cloning Molecular Seawater Amino Acid Sequence Xenopus laevis Gene Expression Regulation Subcellular Fractions/metabolism Protein Transport Sequence Homology Amino Acid Aquaporins/chemistry Animals Intestines/cytology Fluorescent Antibody Technique Intestinal Mucosa/metabolism Organ Specificity/genetics article 2013 ftsydanskunivpub https://doi.org/10.1242/jeb.087890 2024-04-24T00:23:44Z Aquaporins may facilitate transepithelial water absorption in the intestine of seawater (SW)-acclimated fish. Here we have characterized three full-length aqp8 paralogs from Atlantic salmon (Salmo salar). Bayesian inference revealed that each paralog is a representative of the three major classes of aqp8aa, aqp8ab and aqp8b genes found in other teleosts. The permeability properties were studied by heterologous expression in Xenopus laevis oocytes, and the expression levels examined by qPCR, immunofluorescence and immunoelectron microscopy, and immunoblotting of membrane fractions from intestines of SWchallenged smolts. All three Aqp8 paralogs were permeable to water and urea, whereas Aqp8ab and -8b were, surprisingly, also permeable to glycerol. The mRNA tissue distribution of each paralog was distinct, although some tissues such as the intestine showed redundant expression of more than one paralog. Immunofluorescence microscopy localized Aqp8aa(1+2) to intracellular compartments of the liver and intestine, and Aqp8ab and Aqp8b to apical plasma membrane domains of the intestinal epithelium, with Aqp8b also in goblet cells. In a control experiment with rainbow trout, immunoelectron microscopy confirmed abundant labeling of Aqp8ab and -8b at apical plasma membranes of enterocytes in the middle intestine and also in subapical vesicular structures. During SW challenge, Aqp8ab showed significantly increased levels of protein expression in plasma-membraneenriched fractions of the intestine. These data indicate that the Atlantic salmon Aqp8 paralogs have neofunctionalized on a transcriptional as well as a functional level, and that Aqp8ab may play a central role in the intestinal transcellular uptake of water during SW acclimation. Article in Journal/Newspaper Atlantic salmon Salmo salar University of Southern Denmark Research Portal Journal of Experimental Biology |
institution |
Open Polar |
collection |
University of Southern Denmark Research Portal |
op_collection_id |
ftsydanskunivpub |
language |
English |
topic |
Aquaporin Evolution Intestine Neofunctionalization Osmoregulation Salmon Salmo salar/metabolism Cell Membrane Permeability Molecular Sequence Data Gene Expression Profiling Phylogeny RNA Messenger/genetics Time Factors Cloning Molecular Seawater Amino Acid Sequence Xenopus laevis Gene Expression Regulation Subcellular Fractions/metabolism Protein Transport Sequence Homology Amino Acid Aquaporins/chemistry Animals Intestines/cytology Fluorescent Antibody Technique Intestinal Mucosa/metabolism Organ Specificity/genetics |
spellingShingle |
Aquaporin Evolution Intestine Neofunctionalization Osmoregulation Salmon Salmo salar/metabolism Cell Membrane Permeability Molecular Sequence Data Gene Expression Profiling Phylogeny RNA Messenger/genetics Time Factors Cloning Molecular Seawater Amino Acid Sequence Xenopus laevis Gene Expression Regulation Subcellular Fractions/metabolism Protein Transport Sequence Homology Amino Acid Aquaporins/chemistry Animals Intestines/cytology Fluorescent Antibody Technique Intestinal Mucosa/metabolism Organ Specificity/genetics Engelund, Morten Buch Chauvigné, François Christensen, Birgitte M Finn, Roderick N Cerdà, Joan Madsen, Steffen S Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts |
topic_facet |
Aquaporin Evolution Intestine Neofunctionalization Osmoregulation Salmon Salmo salar/metabolism Cell Membrane Permeability Molecular Sequence Data Gene Expression Profiling Phylogeny RNA Messenger/genetics Time Factors Cloning Molecular Seawater Amino Acid Sequence Xenopus laevis Gene Expression Regulation Subcellular Fractions/metabolism Protein Transport Sequence Homology Amino Acid Aquaporins/chemistry Animals Intestines/cytology Fluorescent Antibody Technique Intestinal Mucosa/metabolism Organ Specificity/genetics |
description |
Aquaporins may facilitate transepithelial water absorption in the intestine of seawater (SW)-acclimated fish. Here we have characterized three full-length aqp8 paralogs from Atlantic salmon (Salmo salar). Bayesian inference revealed that each paralog is a representative of the three major classes of aqp8aa, aqp8ab and aqp8b genes found in other teleosts. The permeability properties were studied by heterologous expression in Xenopus laevis oocytes, and the expression levels examined by qPCR, immunofluorescence and immunoelectron microscopy, and immunoblotting of membrane fractions from intestines of SWchallenged smolts. All three Aqp8 paralogs were permeable to water and urea, whereas Aqp8ab and -8b were, surprisingly, also permeable to glycerol. The mRNA tissue distribution of each paralog was distinct, although some tissues such as the intestine showed redundant expression of more than one paralog. Immunofluorescence microscopy localized Aqp8aa(1+2) to intracellular compartments of the liver and intestine, and Aqp8ab and Aqp8b to apical plasma membrane domains of the intestinal epithelium, with Aqp8b also in goblet cells. In a control experiment with rainbow trout, immunoelectron microscopy confirmed abundant labeling of Aqp8ab and -8b at apical plasma membranes of enterocytes in the middle intestine and also in subapical vesicular structures. During SW challenge, Aqp8ab showed significantly increased levels of protein expression in plasma-membraneenriched fractions of the intestine. These data indicate that the Atlantic salmon Aqp8 paralogs have neofunctionalized on a transcriptional as well as a functional level, and that Aqp8ab may play a central role in the intestinal transcellular uptake of water during SW acclimation. |
format |
Article in Journal/Newspaper |
author |
Engelund, Morten Buch Chauvigné, François Christensen, Birgitte M Finn, Roderick N Cerdà, Joan Madsen, Steffen S |
author_facet |
Engelund, Morten Buch Chauvigné, François Christensen, Birgitte M Finn, Roderick N Cerdà, Joan Madsen, Steffen S |
author_sort |
Engelund, Morten Buch |
title |
Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts |
title_short |
Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts |
title_full |
Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts |
title_fullStr |
Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts |
title_full_unstemmed |
Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts |
title_sort |
differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged atlantic salmon smolts |
publishDate |
2013 |
url |
https://portal.findresearcher.sdu.dk/da/publications/19513a81-36e3-4822-8ef2-a65abc627277 https://doi.org/10.1242/jeb.087890 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_source |
Engelund , M B , Chauvigné , F , Christensen , B M , Finn , R N , Cerdà , J & Madsen , S S 2013 , ' Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts ' , Journal of Experimental Biology , vol. 216 , no. 20 , pp. 3873-3885 . https://doi.org/10.1242/jeb.087890 |
op_relation |
https://portal.findresearcher.sdu.dk/da/publications/19513a81-36e3-4822-8ef2-a65abc627277 |
op_rights |
info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1242/jeb.087890 |
container_title |
Journal of Experimental Biology |
_version_ |
1799476950053421056 |