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Fig. 1. Determination of the Ability of Cafestol to Interact with a Range of Nuclear Receptors in Vitro
HepG2 cells were cotransfected with the Gal4 luciferase reporter and a series of chimeras in which the Gal4 DNA-binding domain is fused to the indicated nuclear hormone receptor ligand-binding domain. The cells were treated with a known receptor-specific agonist or 20 µM cafestol. Results are expressed as normalized luciferase activity relative to the known ligand control (set at 100%) (mean ± SEM). Gal4 with cafestol was normalized to the transactivation value obtained with the Gal4-receptor chimera with ligand, which was set at 100%. The ligands used were as follows. Mouse constitutive androstane receptor (mCAR): 250 nM 1,4-bis[2-(3,5-dichloropyridyloxy)]benzene (TCPOBOP); estrogen receptor-
(ER): 1 µM estradiol (E2); FXR: 100 µM CDCA; glucocorticoid receptor (GR): 100 nM dexamethasone; LXR: 1 µM LG101268; peroxisome proliferator-activated receptor (PPAR): 300 nM clofibrate; PPAR
: 1 µM roziglitazone; mPXR: 10 µM PCN; RAR: 1 µM all-trans retinoic acid; RXR: 1 µM 9-cis-retinoic acid; thyroid hormone receptor (TR)ß: 1 µM T3; vitamin D receptor (VDR): 100 nM 1,25-dihydroxyvitamin D3.
