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. Author manuscript; available in PMC: 2016 Apr 1.

Published in final edited form as: Mol Nutr Food Res. 2015 Mar 11;59(4):622–633. doi: 10.1002/mnfr.201400631

3T3-L1 adipocytes were incubated without or with catechin (C), quercetin (Q) or both compounds (CQ) (1 and 10 µM) for 4 h, and subsequently in the absence or presence of 20 ng/ml TNFα for further 24h to measure protein carbonyls, 15 min (MAPKs) or 2 h (AP-1). (A) protein carbonyls were measured as described in methods; (B) phosphorylated and total JNK1/2 and p38 protein levels in total cell extracts; (C) AP-1-DNA binding in nuclear fractions as determined by EMSA. Bands were quantified and results were referred to untreated cell values (Arbitrary unit = 1). For Western blots (B) results were expressed as the ratio phosphorylated/total protein levels. Data represent means ± SEM of three to five independent experiments. Values having different superscripts are significantly different, p < 0.05, one way ANOVA test.

3T3-L1 adipocytes were incubated without or with catechin (C), quercetin (Q) or both compounds (CQ) (1 and 10 µM) for 4 h, and subsequently in the absence or presence of 20 ng/ml TNFα for further 24h to measure protein carbonyls, 15 min (MAPKs) or 2 h (AP-1). (A) protein carbonyls were measured as described in methods; (B) phosphorylated and total JNK1/2 and p38 protein levels in total cell extracts; (C) AP-1-DNA binding in nuclear fractions as determined by EMSA. Bands were quantified and results were referred to untreated cell values (Arbitrary unit = 1). For Western blots (B) results were expressed as the ratio phosphorylated/total protein levels. Data represent means ± SEM of three to five independent experiments. Values having different superscripts are significantly different, p < 0.05, one way ANOVA test.