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Am J Physiol Regul Integr Comp Physiol 294: R1367-R1378, 2008. First published February 6, 2008; doi:10.1152/ajpregu.00454.2007
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WATER AND ELECTROLYTE HOMEOSTASIS

Identification of FXYD protein genes in a teleost: tissue-specific expression and response to salinity change

Christian Kølbæk Tipsmark

Institute of Biology, University of Southern Denmark, Odense, Denmark

Submitted 26 June 2007 ; accepted in final form 1 February 2008

It is increasingly clear that alterations in Na+-K+-ATPase kinetics to fit the demands in specialized cell types is vital for the enzyme to execute its different physiological roles in diverse tissues. In addition to tissue-dependent expression of isoforms of the conventional subunits, {alpha} and β, auxiliary FXYD proteins appear to be essential regulatory components. The present study identified genes belonging to this family in Atlantic salmon by analysis of expressed sequence tags. Based on the conserved domain of these small membrane proteins, eight expressed FXYD isoforms were identified. Phylogenetic analysis suggests that six isoforms are homologues to the previously identified FXYD2, FXYD5, FXYD6, FXYD7, FXYD8, and FXYD9, while two additional isoforms were found (FXYD11 and FXYD12). Using quantitative PCR, tissue-dependent expression of the different isoforms was analyzed in gill, kidney, intestine, heart, muscle, brain, and liver. Two isoforms were expressed in several tissues (FXYD5 and FXYD9), while six isoforms were distributed in a discrete manner. In excitable tissues, two isoforms were highly expressed in brain (FXYD6 and FXYD7) and one in skeletal muscle (FXYD8). In osmoregulatory tissues, one isoform was expressed predominantly in gill (FXYD11), one in kidney (FXYD2), and one equally in kidney and intestine (FXYD12). Expression of several FXYD genes in kidney and gill differed between fresh water and seawater salmon, suggesting significance during osmoregulatory adaptations. In addition to identifying novel FXYD isoforms, these studies are the first to show the tissue dependence in their expression and modulation by salinity in any teleosts.

Atlantic salmon; sodium-potassium-adenosinediphosphatase; osmoregulation; Salmo salar; quantitative polymerase chain reaction



Address for reprint requests and other correspondence: C. K. Tipsmark, Institute of Biology, Univ. of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark (e-mail: ckt{at}biology.sdu.dk.)




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