English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The European eel is a euryhaline teleost which has been shown to differentially up- and downregulate aquaporin (AQP) water channels in response to changes in environmental salinity. We have characterized the transport properties of four aquaporins localized to osmoregulatory organs - gill, esophagus, intestine and kidney. By sequence comparison these four AQP orthologs resemble human AQP1 (eel AQP1), AQP3 (eel AQP3) and AQP10 (AQPe). The fourth member is a duplicate form of AQP1 (AQP1dup) thought to arise from a duplication of the teleost genome. Using heterologous expression in Xenopus oocytes we demonstrate that all four eel orthologs transport water and are mercury inhibitable. Eel AQP3 and AQPe also transport urea and glycerol, making them aquaglyceroporins. Eel AQP3 is dramatically inhibited by extracellular acidity (91% and 69% inhibition of water and glycerol transport respectively at pH 6.5) consistent with channel gating by protons. Maximal water flux of eel AQP3 occurred around pH 8.2 - close to the physiological pH of plasma in the eel. Exposure of AQP-expressing oocytes to heavy metals revealed that eel AQP3 is highly sensitive to extracellular nickel and zinc (88.3% and 86.3% inhibition, respectively) but less sensitive to copper (56.4% inhibition). Surprisingly, copper had a stimulatory effect on eel AQP1 (153.7% activity of control). Copper, nickel and zinc did not affect AQP1dup or AQPe. We establish that all four eel AQP orthologs have similar transport profiles to their human counterparts, with eel AQP3 exhibiting some differences in its sensitivity to metals. This is the first investigation of the transport properties and inhibitor sensitivity of salinity-regulated aquaporins from a euryhaline species. Our results indicate a need to further investigate the deleterious effects of metal pollutants on AQP-containing epithelial cells of the gill and gastrointestinal tract at environmentally appropriate concentrations.

Expression and functional characterization of four aquaporin water channels from the European eel (Anguilla anguilla)