Literature DB >> 17126580

The role of aquaporin 3 in teleost fish.

Christopher Paul Cutler1, Anne-Sophie Martinez, Gordon Cramb.   

Abstract

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 splicoform/isoform has also been identified in rainbow trout (Oncorhynchus mykiss). The identification of these AQP3 isoforms in other fish species is consequently explored. The role of AQP3 in physiological/osmoregulatory processes, in various teleost organs is then described. In teleost gill, AQP3 is expressed in 'chloride' cells, and in some species, in other epithelial cell types, where it may have a number of different functions including the prevention of dehydration. In eel esophagus, immunohistochemistry shows that AQP3 is expressed in surface epithelial cells in the anterior esophagus, but in mucus cells within the epithelium of the posterior esophagus. In eel intestine, AQP3 is found in macrophage-like cells and probably plays no part in osmoregulatory processes. In the rectum, as in the posterior esophagus AQP3 is expressed in mucus cells. In eel kidney, AQP3 is expressed in a subset of renal tubules, and localizes to the apical pole of tubule cells. There is no apparent change in the location or protein abundance of renal AQP3 following the acclimation of eels from freshwater to seawater.

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Year:  2006        PMID: 17126580     DOI: 10.1016/j.cbpa.2006.09.022

Source DB:  PubMed          Journal:  Comp Biochem Physiol A Mol Integr Physiol        ISSN: 1095-6433            Impact factor:   2.320


  32 in total

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Review 4.  Osmoregulation in fish sperm.

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Review 5.  The physiology of hyper-salinity tolerance in teleost fish: a review.

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8.  The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate specificities similar to mammals.

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9.  Morphological and molecular evidence for functional organization along the rostrocaudal axis of the adult zebrafish intestine.

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