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Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: Three peroxisome proliferator-activated receptor isotypes from each of two species of marine fish
Authors: Leaver, Michael
Boukouvala, Evridiki
Antonopoulou, Efthimia
Diez, Amalia
Favre-Krey, Laurence
Ezaz, M Tariq
Bautista, Jose M
Tocher, Douglas R
Krey, Grigorios
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Issue Date: Jul-2005
Publisher: The Endocrine Society
Citation: Leaver M, Boukouvala E, Antonopoulou E, Diez A, Favre-Krey L, Ezaz MT, Bautista JM, Tocher DR & Krey G (2005) Three peroxisome proliferator-activated receptor isotypes from each of two species of marine fish, Endocrinology, 146 (7), pp. 3150-3162.
Abstract: 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 PPARα, PPARβ/δ, and PPARγ. 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, PPARγ is expressed more widely in fish tissues than in mammals, whereas PPARα and β 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 PPARα and β exhibit an activation profile similar to that of the mammalian PPAR in response to a variety of activators/ligands, whereas PPARγ is not activated by mammalian PPARγ-specific ligands. Amino acid residues shown to be critical for ligand binding in mammalian PPARs are not conserved in fish PPARγ and therefore, together with the distinct tissue expression profile of this receptor, suggest potential differences in the function of PPARγ in fish compared
Type: Journal Article
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Rights: Publisher policy allows this work to be made available in this repository.
Affiliation: Aquaculture
National Agricultural Research Foundation
National Agricultural Research Foundation
Universidad Complutense de Madrid
National Agricultural Research Foundation
University of Stirling
Universidad Complutense de Madrid
National Agricultural Research Foundation

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