The role of aquaporin 3 in teleost fish.

TitleThe role of aquaporin 3 in teleost fish.
Publication TypeJournal Article
Year of Publication2007
AuthorsCutler, C, Martinez, A-S, Cramb, G
JournalComp Biochem Physiol A Mol Integr Physiol
Volume148
Issue1
Pagination82-91
Date Published2007 Sep
ISSN1095-6433
KeywordsAmino Acid Sequence, Animals, Aquaporin 3, Esophagus, Fishes, Intestines, Kidney, Molecular Sequence Data, Rectum, Sequence Homology, Amino Acid, Water-Electrolyte Balance
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.

DOI10.1016/j.cbpa.2006.09.022
Alternate JournalComp. Biochem. Physiol., Part A Mol. Integr. Physiol.
PubMed ID17126580