Cloning and expression of three aquaporin homologues from the European eel (<i>Anguilla anguilla</i>): effects of seawater acclimation and cortisol treatment on renal expression

Martinez, Anne‐Sophie; Cutler, Christopher P.; Wilson, Gillian D.; Phillips, Clair; Hazon, Neil; Cramb, Gordon

doi:10.1042/bc20040111

Cited by 67 publications

(84 citation statements)

References 47 publications

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“…Very recent work (reviewed by Cerda and Finn, 2010;Grosell, 2011a) shows that many different aquaporins are widely expressed in the intestinal tract of euryhaline teleosts, and that AQP1 in particular may play a role in water absorption. Observations of elevated mRNA expression following seawater transfer, elevated AQP1 protein abundance in intestinal tissue following seawater acclimation and, finally, apical as well as basolateral localization of the protein suggest a role in transepithelial water movement (Aoki et al, 2003;Martinez et al, 2005a;Martinez et al, 2005b;Raldua et al, 2008). It has been demonstrated that AQP1 genes from fish confer water permeability in expression systems (MacIver et al, 2009), including AQP1a from F. heteroclitus (Tingaud-Sequeira et al, 2009), but despite the above observations, direct evidence for a role for AQP1 in intestinal water absorption has been lacking.…”

Section: A Role For Aquaporins In Intestinal Water Absorption In Fishmentioning

confidence: 99%

Independence of net water flux from paracellular permeability in the intestine ofFundulus heteroclitus, a euryhaline teleost

Wood

Grosell

2012

Journal of Experimental Biology

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SUMMARYParacellular permeability and absorptive water flux across the intestine of the euryhaline killifish were investigated using in vitro gut sac preparations from seawater-and freshwater-acclimated animals. The permeability of polyethylene glycol (PEG), a wellestablished paracellular probe, was measured using trace amounts of radiolabelled oligomers of three different molecular sizes (PEG-400, PEG-900 and PEG-4000) at various times after satiation feeding. All three PEG molecules were absorbed, with permeability declining as a linear function of increasing hydrodynamic radius. Response patterns were similar in seawater and freshwater preparations, though water absorption and PEG-900 permeability were greater in the latter. Despite up to 4-fold variations in absorptive water flux associated with feeding and fasting (highest at 1-3h, lowest at 12-24h and intermediate at 1-2weeks post-feeding), there were no changes in PEG permeability for any size oligomer. When PEG permeability was measured in the opposite direction (i.e. serosal to mucosal) from net water flux, it was again unchanged. HgCl 2 (10 -3 moll -1 ), a putative blocker of aquaporins, eliminated absorptive water flux yet increased PEG-4000 permeability by 6-to 8-fold in both freshwater and seawater preparations. Experimentally raising the serosal osmolality by addition of 300mmoll -1 mannitol increased the absorptive water flux rate 10-fold, but did not alter PEG permeability. Under these conditions, HgCl 2 reduced absorptive water flux by 60% and again increased PEG permeability by 6-to 8-fold in both freshwater and seawater preparations. Clearly, there was no influence of solvent drag on PEG movement. The putative paracellular blocker 2,4,6-triaminopyrimidine (TAP, 20mmoll -1 ) had no effect on net water flux or PEG permeability. We conclude that PEG and water move by separate pathways; absorptive water transport probably occurs via a transcellular route in the intestine of Fundulus heteroclitus.

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Section: A Role For Aquaporins In Intestinal Water Absorption In Fishmentioning

confidence: 99%

Independence of net water flux from paracellular permeability in the intestine ofFundulus heteroclitus, a euryhaline teleost

Wood

Grosell

2012

Journal of Experimental Biology

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“…Previous studies of European eels, Anguilla anguilla, and Atlantic salmon similarly found that the mRNA expression of AQP3 and AQP8 significantly increased during increasing exposure to SW (Martinez et al 2005;Tipsmark et al 2010). Choi et al (2013) found that parr and smolt stage sockeye salmon exposed to SW had an increased expression of AQP3 and AQP8 mRNA and protein in the osmoregulatory organs, such as the gills and the intestine.…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have shown that AQPs are important in the movement of water in euryhaline teleosts (Choi et al 2013;Kim et al 2014;Martinez et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Effects of Recombinant Aquaporin 3 and Seawater Acclimation on the Expression of Aquaporin 3 and 8 mRNAs in the Parr and Smolt Stages of Rainbow Trout, Oncorhynchus mykiss

Kim¹,

Choi²,

Lim³

et al. 2016

Ocean and Polar Research

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: This study aimed to examine the role of two aquaporin isoforms (AQP3 and AQP8) in response to the hyperosmotic challenge of transitioning from freshwater (FW) to seawater (SW) during parr and smoltification (smolt) using the rainbow trout, Oncorhynchus mykiss. We examined the changes in the expression of AQPs mRNAs in the gills and intestine of the parr and smolt stages of rainbow trout transferred from FW to SW using quantitative real-time PCR in an osmotically changing environment [FW, SW, and recombinant AQP3 (rAQP3) injection at two dosage rates]. Correspondingly, AQPs were greater during smoltification than during parr stages in the rainbow trout. Plasma osmolality and gill Na + /K + -ATPase activity increased when the fish were exposed to SW, but these parameters decreased when the fish were exposed to SW following treatment with rAQP3 during the transition to seawater. Our results suggest that AQPs play an important role in water absorbing mechanisms associated with multiple AQP isoforms in a hyperosmotic environment.

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“…Although there is some consensus on the expression pattern of each paralog, there is emerging evidence that even closely related aquaporins, such as the tandemly duplicated aqp1aa and aqp1ab genes and alternatively duplicated aqp8 paralogs, have neofunctionalized in relation to their regulation and function (Martinez et al, 2005a;Martinez et al, 2005b;Tipsmark et al, 2010;Madsen et al, 2011;Finn and Cerdà, 2011;Zapater et al, 2011). In the stenohaline FW zebrafish, aqp8 is present as three paralogs (aqp8aa, -8ab and -8b) and fragments of each have been found in a partial transcriptome (EST library) of the Atlantic salmon (Tingaud-Sequeira et al, 2010;Cerdà and Finn, 2010;Engelund and Madsen, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…To date, the piscine aquaporin superfamily has only been characterized in the diploid zebrafish (Danio rerio) (TingaudSequeira et al, 2010), while other species of teleost have been examined with respect to basal expression patterns of selected aquaporins within osmoregulatory tissues Lignot et al, 2002;Martinez et al, 2005a;Martinez et al, 2005b;Raldúa et al, 2008;Tingaud-Sequeira et al, 2010;Tipsmark et al, 2010;Madsen et al, 2011). Although there is some consensus on the expression pattern of each paralog, there is emerging evidence that even closely related aquaporins, such as the tandemly duplicated aqp1aa and aqp1ab genes and alternatively duplicated aqp8 paralogs, have neofunctionalized in relation to their regulation and function (Martinez et al, 2005a;Martinez et al, 2005b;Tipsmark et al, 2010;Madsen et al, 2011;Finn and Cerdà, 2011;Zapater et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts

Engelund

Chauvigné

Christensen

et al. 2013

Journal of Experimental Biology

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SUMMARYAquaporins 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. Supplementary material available online at

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Cloning and expression of three aquaporin homologues from the European eel (Anguilla anguilla): effects of seawater acclimation and cortisol treatment on renal expression

Cited by 67 publications

References 47 publications

Independence of net water flux from paracellular permeability in the intestine ofFundulus heteroclitus, a euryhaline teleost

Independence of net water flux from paracellular permeability in the intestine ofFundulus heteroclitus, a euryhaline teleost

Effects of Recombinant Aquaporin 3 and Seawater Acclimation on the Expression of Aquaporin 3 and 8 mRNAs in the Parr and Smolt Stages of Rainbow Trout, Oncorhynchus mykiss

Differential expression and novel permeability properties of three aquaporin 8 paralogs from seawater-challenged Atlantic salmon smolts

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