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The Preservation of PPAR¿ Genome Duplicates in Some Teleost Lineages: Insights into Lipid Metabolism and Xenobiotic Exploitation

Title
The Preservation of PPAR¿ Genome Duplicates in Some Teleost Lineages: Insights into Lipid Metabolism and Xenobiotic Exploitation
Type
Article in International Scientific Journal
Year
2022
Authors
Páscoa, I
(Author)
Other
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Fonseca, E
(Author)
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Ferraz, R
(Author)
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Machado, AM
(Author)
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Conrado, F
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Ruivo, R
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Cunha, I
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Filipe F C Castro
(Author)
FCUP
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Journal
Title: GenesImported from Authenticus Search for Journal Publications
Vol. 13
Final page: 107
ISSN: 2073-4425
Publisher: MDPI
Indexing
Other information
Authenticus ID: P-00W-2A9
Abstract (EN): Three peroxisome proliferator-activated receptor paralogues (PPAR¿,-ß and-¿) are currently recognized in vertebrate genomes. PPAR¿ is known to modulate nutrition, adipogenesis and immunity in vertebrates. Natural ligands of PPAR¿ have been proposed; however, the receptor also binds synthetic ligands such as endocrine disruptors. Two paralogues of PPAR¿ and PPARß have been documented in teleost species, a consequence of the 3R WGD. Recently, two PPAR¿ paralogue genes were also identified in Astyanax mexicanus. We aimed to determine whether the presence of two PPAR¿ paralogues is prevalent in other teleost genomes, through genomic and phylogenetic analysis. Our results showed that besides Characiformes, two PPAR¿ paralogous genes were also identified in other teleost taxa, coinciding with the teleost-specific, whole-genome duplication and with the retention of both genes prior to the separation of the Clupeocephala. To functionally characterize these genes, we used the European sardine (Sardina pilchardus) as a model. PPAR¿A and PPAR¿B display a different tissue distribution, despite the similarity of their functional profiles: they are unresponsive to tested fatty acids and other human PPAR¿ ligands yet yield a transcriptional response in the presence of tributyltin (TBT). This observation puts forward the relevance of comparative analysis to decipher alternative binding architectures and broadens the disruptive potential of man-made chemicals for aquatic species. © 2022 by the authors. Licensee MDPI, Basel, Switzerland.
Language: English
Type (Professor's evaluation): Scientific
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