Christopher Paul Cutler

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The dynamics of branchial Na(+),K(+),2Cl(-) cotransporter (NKCC) and Na(+),K(+)-ATPase (NKA) expression were investigated in brown trout and Atlantic salmon during salinity shifts and the parr-smolt transformation, respectively. In the brown trout, Western blotting revealed that NKCC and NKA abundance increased gradually and in parallel (30- and ten-fold,(More)
A cDNA encoding the homologue of mammalian aquaporin 3 (AQP-3) was isolated by reverse transcription-polymerase chain reaction from the gill of the European eel. The derived amino acid sequence shares 67-70% homology with other vertebrate AQP-3 homologues. Northern blot analysis revealed two AQP-3-specific mRNA species of 2.4 kb and 7 kb. AQP-3 mRNA is(More)
BACKGROUND INFORMATION The European eel (Anguilla anguilla) is able to osmoregulate over a wide range of environmental salinities from FW (freshwater) to hyperconcentrated SW (seawater). Successful acclimation is associated with strict regulation of ion and water transport pathways within key osmoregulatory epithelia to enable animals to survive the(More)
Two cDNA isoforms of the NKCC1 secretory cotransporter have been isolated from the European eel. The NKCC1a isoform exhibited mRNA expression in a wide range of tissues in a similar fashion to mammals, whereas NKCC1b was expressed primarily in the brain. The effect of freshwater (FW) to seawater (SW) transfer on NKCC1a expression was dependent on the(More)
The aquaporin isoform, AQP3 has now been identified in a number of different teleost fish species, with additional DNA sequence information on AQP3 genes in further fish species available in genome databases. In zebrafish (Danio rerio), the AQP3 gene is present as two duplicate isoforms resulting from a teleostean fish genome-wide duplication. A further(More)
Complementary DNAs encoding homologs of the mammalian aquaglyceroporins (termed AQPe) and aquaporin-1 isoforms (termed AQP1) were isolated from the European eel. The AQP amino acid sequences share 35-54% identity with other known human AQPs. Although AQPe mRNA expression was approximately equivalent along the entire length of the gut, AQP1 expression was(More)
The entire amino acid coding sequence of the Na+,K+-ATPase β1 isoform was cloned from the gill of the European eel (Anguilla anguilla) by a PCR based method. The amino acid sequence translated from the nucleotide sequence shared 61.4 and 56.2% homology respectively with previously published Na+,K+-ATPase β1 isoform sequences from the clawed toad (Xenopus(More)
The expression of a putative water channel protein, aquaporin 3 (AQP-3), has been localised within branchial and intestinal tissues from the 'silver' life stage of the European eel Anguilla anguilla, using a specific polyclonal antibody directed against the C-terminal of the amino acid sequence. Western blots using the AQP-3 antiserum identified the(More)
This review focuses on recent developments in the molecular biology of ion and water transporter genes in fish and the potential role of their products in osmoregulation in both freshwater and seawater environments. In particular details of isoforms of various ATPases, co-transporters, exchangers and ion channels in the eel as well as other teleost species(More)
In Na,K-ATPase membrane preparations from shark rectal glands, we have previously identified an FXYD domain-containing protein, phospholemman-like protein from shark, PLMS. This protein was shown to associate and modulate shark Na,K-ATPase activity in vitro. Here we describe the complete coding sequence, expression, and cellular localization of PLMS in the(More)