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Three Peroxisome Proliferator-Activated Receptor Isotypes from Each of Two Species of Marine Fish

Institute of Aquaculture (M.J.L., M.T.E., D.R.T.), University of Stirling, Stirling FK9 4LA, United Kingdom; National Agricultural Research Foundation (E.B., E.A., L.F.-K., G.K.), Fisheries Research Institute, Nea Peramos, 64007 Kavala, Greece; and Departamento de Bioquimica y Biologia Molecular IV (A.D., J.M.B.), Facultad de Veterinaria, Universidad Complutense de Madrid, 28040 Madrid, Spain

Address all correspondence and requests for reprints to: Grigorios Krey, National Agricultural Research Foundation, Fisheries Research Institute, Nea Peramos, 64007 Kavala, Greece. E-mail: krey{at}otenet.gr.

The cloning and characterization of cDNAs and genes encoding three peroxisome proliferator-activated receptor (PPAR) isotypes from two species of marine fish, the plaice (Pleuronectes platessa) and the gilthead sea bream (Sparus aurata), are reported for the first time. Although differences in the genomic organization of the fish PPAR genes compared with their mammalian counterparts are evident, sequence alignments and phylogenetic comparisons show the fish genes to be homologs of mammalian PPAR, PPARß/, and PPAR. Like their mammalian homologs, fish PPARs bind to a variety of natural PPAR response elements (PPREs) present in the promoters of mammalian or piscine genes. In contrast, the mRNA expression pattern of PPARs in the two fish species differs from that observed in other vertebrates. Thus, PPAR is expressed more widely in fish tissues than in mammals, whereas PPAR and ß are expressed similarly in profile to mammals. Furthermore, nutritional status strongly influences the expression of all three PPAR isotypes in liver, whereas it has no effect on PPAR expression in intestinal and adipose tissues. Fish PPAR and ß exhibit an activation profile similar to that of the mammalian PPAR in response to a variety of activators/ligands, whereas PPAR is not activated by mammalian PPAR-specific ligands. Amino acid residues shown to be critical for ligand binding in mammalian PPARs are not conserved in fish PPAR and therefore, together with the distinct tissue expression profile of this receptor, suggest potential differences in the function of PPAR in fish compared with mammals.

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