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Structural Features and Transcriptional Activity of Chicken PPARs (α,β, andγ)
Author(s) -
Ichiro Takada,
Mime Kobayashi
Publication year - 2013
Publication title -
ppar research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 49
eISSN - 1687-4765
pISSN - 1687-4757
DOI - 10.1155/2013/186312
Subject(s) - transactivation , lipid metabolism , gene isoform , luciferase , gene , metabolism , peroxisome proliferator activated receptor , biology , function (biology) , biochemistry , microbiology and biotechnology , gene expression , genetics , transfection
While an understanding of lipid metabolism in chickens is critical for a further improvement of food production, there are few studies concerning differences in lipid metabolism mechanisms between chickens and other species at a molecular level. Chickens have three PPAR gene subtypes ( α , β , and γ ) that function differently from those present in humans and mice. The chicken PPAR-gamma (cPPAR γ ) gene is shorter than that in humans and lacks a γ 2 isoform. Moreover, in serum-free media, cPPAR γ shows high transcriptional activity without exogenous ligands. Luciferase reporter assays were used to examine the effect of sera on cPPAR transcriptional activities and showed that adult bovine serum and chicken serum highly activate cPPAR α and β functions. Moreover, we found that bezafibrate induces the transactivation function of cPPAR β , but not human PPAR δ (human PPAR β ortholog). This ligand selectivity relies on one amino acid residue (chicken: Val419, human: Met444). These results show the possibilities for unique functions of cPPARs on chicken-specific lipid glucose metabolism. As such, a better understanding of the molecular mechanisms of lipid metabolism in chickens could result in higher productivity for the poultry industry.

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