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Institute of Aquaculture, University of Stirling, Stirling FK9 4LA, UK
¹ National Agricultural Research Foundation, Fisheries Research Institute, Nea Peramos, 64007 Kavala, Greece

(Requests for offprints should be addressed to M J Leaver; Email: mjl1{at}stir.ac.uk)

(M Tariq Ezaz is now at Research School of Biological Sciences, Australian National University, Canberra, Australian Capital Territory 0200, Australia)
(S Fontagne is now at INRA, 64310 Saint-Pee sur Nivelle, France)

Peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors belonging to the nuclear hormone receptor superfamily that functions as critical regulators of lipid and energy homeostasis. Although intensively studied in mammals, their basic biological functions are still poorly understood. The objective of this work was to characterize PPARß subtypes in a fish, the Atlantic salmon (Salmo salar), in order to address PPAR function and the regulation of lipid homeostasis in lower vertebrates. The screening of an Atlantic salmon genomic library revealed the presence of four genes for PPARß subtypes. Based on comparisons of exons and exon-flanking regions, these genes were assigned into two families, ssPPARß1 and ssPPARß2, each family containing two isotypes: ssPPARß1A and ß1B and ssPPARß2A and ß2B. Two full-length cDNAs for ssPPARß1A and ssPPPARß2A were isolated. Transcripts for ssPPARß1A and ssPPARß2A have distinct tissue expression profiles, with ssPPARß1A predominating in liver and ssPPARß2A predominating in gill. Expression levels of mRNA of either isotypes were up to tenfold lower in kidney, heart, spleen, muscle, and brain. In cellular transfection assays, ssPPARß1A is activated by monounsaturated fatty acids, 2-bromopalmitate, and mammalian PPARß-specific ligand GW501516. In contrast, PPARß2A was not activated by any of the compounds tested. Furthermore, ssPPARß2A repressed both the basal reporter gene activity and the GW501516-induced activity of ssPPARß1A. The results indicate unexpected levels of variety and complexity in PPAR subtype and mechanism of action in lower vertebrates.

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