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The DNA and ligand binding properties of fish PPARs

The DNA binding properties of the PPAR isotypes from plaice, sea bream, Atlantic salmon, and sea bass have been studied by the electrophoretic mobility shift assay (EMSA) using in vitro translated PPAR proteins and a variety of PPAR response elements of both mammalian and piscine origin. This result demonstrates that fish PPARs, like their mammalian homologues heterodimerize with RXR and recognize response elements of the DR-1 type.

The ligand binding properties of the fish PPARs were studied through the coactivator-dependent receptor ligand assay (CARLA) and it was demonstrated that fatty acids, eicosanoids, and synthetic hypolipidemic drugs can induce the interactions of the ligand binding domain of the receptors with the mammalian steroid receptor coactivator-1(SRC-1).

The above, besides establishing the DNA and ligand binding properties of the fish PPARs also demonstrate that the mechanisms involved in PPAR transactivation have evolved before the divergence of the osteichthyan and mammalian lieages. Therefore, further optimization of the CARLA assay could result in the identification of novel ligands for the fish PPARs with potential use in commercial fish feeds.

An important finding is the identification of conjugated linoleic acid (CLA) as fish PPAR ligand that has been applied in experimental fish diets with promising results.

Reported by

National Agricultural Research Foundation-Fisheries Research Institute
Nea Peramos
64007 Kavala
Greece
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