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. Author manuscript; available in PMC: 2012 Aug 1.
Published in final edited form as: Cell Signal. 2011 Apr 9;23(8):1396–1403. doi: 10.1016/j.cellsig.2011.03.023

Fig. 5.

Fig. 5

Reducing cytoplasmic RIP140 in adipocytes suppresses the inflammatory properties of their conditioned media. (A) Silencing RIP140 or PKCε in adipocytes reduces the ability of the conditioned media to activate NF-κB activity in cultured Raw264.7 macrophages. *: p value < 0.05 compared to the control siRNA in the control group. **: p value < 0.05 compared to the control siRNA in the isoproterenol group. (B) Silencing RIP140 or PKCε in 3T3-L1 adipocytes reduces the ability of their conditioned media to activate expression of endogenous proinflammatory genes in Raw264.7. *: p value < 0.05 compared to the control group of IL-1 beta. **: p value < 0.05 compared to the control group of IL-6. (C) Schematic presentation of the role of cytoplasmic RIP140 in modulating lipolysis in adipocytes. After HFD feeding, the DAG-PKCε signaling cascade promotes nuclear export of RIP140. Cytoplasmic RIP140 then interacts with perilipin to enhance lipolysis by promoting the formation of perilipin-HSL and ATGL/CGI-58 complexes.