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. Author manuscript; available in PMC: 2014 Jul 5.
Published in final edited form as: Biochem Pharmacol. 2011 Jul 30;82(12):1807–1821. doi: 10.1016/j.bcp.2011.07.093

Fig. 3. Possible modulation of NF-kB pathway by EGCG.

Fig. 3

In the cytosol as a result of the binding of p50 and p65 to I-kB, NF-kB becomes inactive. When I-kB is phosphorylated by IKKs and degraded in a proteasome-dependent pathway, p50 and p65 are set free and are translocated into the nucleus to activate a specific set of genes. In vitro and in vivo this pathway has been shown to be inhibited by EGCG both, possibly by inhibiting IKK-catalyzed phosphorylation of I-kB.