Curcumin is not a ligand for peroxisome proliferator-activated receptor-γ

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Date
2009-12-01
Authors
Narala, Venkata R.
Smith, Monica R.
Adapala, Ravi K.
Ranga, Rajesh
Panati, Kalpana
Moore, Bethany B.
Leff, Todd
Reddy, Vudem D.
Kondapi, Anand K.
Reddy, Raju C.
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Abstract
Curcumin, a compound found in the spice turmeric, has been shown to possess a number of beneficial biological activities exerted through a variety of different mechanisms. Some curcumin effects have been reported to involve activation of the nuclear transcription factor peroxisome proliferator-activated receptor-γ (PPAR-γ), but the concept that curcumin might be a PPAR-γ ligand remains controversial. Results reported here demonstrate that, in contrast to the PPAR-γ ligands ciglitazone and rosiglitazone, curcumin is inactive in five different reporter or DNAbinding assays, does not displace [3H]rosiglitazone from the PPAR-γ ligand-binding site, and does not induce PPAR-γ-dependent differentiation of preadipocytes, while its ability to inhibit fibroblast-to-myofibroblast differentiation is not affected by any of four PPAR-γ antagonists. These multiple lines of evidence conclusively demonstrate that curcumin is not a PPAR-γ ligand and indicate the need for further investigation of the mechanisms through which the compound acts.
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Keywords
Ciglitazone, Curcumin, Fibroblast, Peroxisome, PPAR-γ, PPRE, Preadipocyte, Rosiglitazone, TGF-β, Turmeric
Citation
Gene Therapy and Molecular Biology. v.13(1)