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Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: Molecular characterization of three peroxisome proliferator-activated receptors from the sea bass (Dicentrarchus labrax)
Authors: Boukouvala, Evridiki
Antonopoulou, Efthimia
Favre-Krey, Laurence
Diez, Amalia
Bautista, Jose M
Leaver, Michael
Tocher, Douglas R
Krey, Grigorios
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Issue Date: Nov-2004
Publisher: Springer
Citation: Boukouvala E, Antonopoulou E, Favre-Krey L, Diez A, Bautista JM, Leaver M, Tocher DR & Krey G (2004) Molecular characterization of three peroxisome proliferator-activated receptors from the sea bass (Dicentrarchus labrax), Lipids, 39 (11), pp. 1085-1092.
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 mammal
Type: Journal Article
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Affiliation: National Agricultural Research Foundation
National Agricultural Research Foundation
National Agricultural Research Foundation
Universidad Complutense de Madrid
Universidad Complutense de Madrid
National Agricultural Research Foundation

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