Molecular characterization of three peroxisome proliferator-activated receptors from the sea bass (<Emphasis Type="Italic">Dicentrarchus labrax</Emphasis>) |
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Authors: | Evridiki?Boukouvala Efthimia?Antonopoulou Laurence?Favre-Krey Amalia?Diez José?M?Bautista Michael?J?Leaver Douglas?R?Tocher Email author" target="_blank">Grigorios?KreyEmail author |
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Affiliation: | (1) National Agricultural Research Foundation-Fisheries Research Institute, Nea Peramos, 64007 Kavala, Greece;(2) Departamento de Bioquimica y Biologia Molecular IV, Facultad de Veterinaria, Universidad Complutenses de Madrid, 28040 Madrid, Spain;(3) Institute of Aquaculture, University of Stirling, FK9 4LA Stirling, Scotland;(4) Present address: Department of Biology, Laboratory of Physiology, Aristotelio University of Thessaloniki, GR-54124 Thessaloniki, GR |
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Abstract: | Peroxisome proliferator-activated receptors (PPAR) are nuclear hormone receptors that control the expression of genes involved
in lipid homeostasis in mammals. We searched for PPAR in sea bass, a marine fish of particular interest to aquaculture, after
hypothesizing that the physiological and molecular processes that regulate lipid metabolism in fish are similar to those in
mammals. Here, we report the identification of complementary DNA and corresponding genomic sequences that encode three distinct
PPAR from sea bass. The sea bass PPAR are the structural homologs of the mammalian PPARα, β/δ and γ isotypes. As revealed
by RNase protection, the tissue expression profile of the fish PPAR appears to be very similar to that of the mammalian PPAR
homologs. Thus, PPARα is mainly expressed in the liver, PPARγ in adipose tissue, and PPARβ in all tissues tested, with its
highest levels in the liver, where it is also the dominant isotype expressed. Like mammalian PPAR, the sea bass isotypes recognize
and bind to PPAR response elements of both mammalian and piscine origin, as heterodimers with the 9-cis retinoic acid receptor. Through the coactivator-dependent receptor ligand assay, we also demonstrated that natural FA and
synthetic hypolipidemic compounds can act as ligands of the sea bass PPARα and β isotypes. This suggests that the sea bass
PPAR act through similar mechanisms and perform the same critical lipid metabolism functions as mammalian PPAR. |
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