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• W2085806036 abstract "The peroxisome proliferator-activated receptors (PPARs) bind and are activated by a variety of fatty acids and derivatives thereof. Agonist binding enhances PPAR-mediated transactivation via release of corepressors and recruitment of coactivator complexes. Recently, we and others have reported that acyl-CoA esters act as PPAR antagonists in vitro. Here, we show that the binding of the nonhydrolyzable acyl-CoA analogue, S-hexadecyl-CoA, differentially affected conformation and coactivator recruitment of the individual PPAR subtypes. In protease protection assays, S-hexadecyl CoA increased the sensitivity of PPARalpha and PPARdelta towards chymotrypsin, whereas the action of chymotrypsin on PPARgamma was only marginally affected, suggesting distinct subtype-dependent differences in the effects of S-hexadecyl-CoA on conformation of the PPARs. In keeping with these findings, S-hexadecyl-CoA abrogated ligand-induced recruitment of coactivators to PPARalpha and PPARdelta, whereas coactivator recruitment to PPARgamma was unaffected by S-hexadecyl-CoA." @default.
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• W2085806036 date "2002-06-01" @default.
• W2085806036 modified "2023-09-23" @default.
• W2085806036 title "Opposing Effects of Fatty Acids and Acyl-CoA Esters on Conformation and Cofactor Recruitment of Peroxisome Proliferator-Activated Receptors" @default.
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• W2085806036 doi "https://doi.org/10.1111/j.1749-6632.2002.tb04299.x" @default.
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