Inhibition of Proteasome Activity Upregulates IL-6 Expression in RPE Cells through the Activation of P38 MAPKs

Figure 3

Proteasome inhibitor (MG132, 10 μM) can activate p38 MAPK and JNK in RPE. (a) ARPE-19 cells were cultured in the absence or presence of the proteasome inhibitor MG132 (10 μM) for 1, 2, 4, and 8 h. Levels of endogenous phospho-p38 MAPK, total p38 MAPK, and actin were detected by Western blot using polyclonal (to phosphorylated and total p38 MAPK) and monoclonal antibodies (to actin). Is the only one phosphorylated site of P38 MAPK. (b) ARPE-19 cells were cultured in the absence or presence of the proteasome inhibitor MG132 (10 μM) for 1, 2, 4, and 8 h. Levels of endogenous phospho-JNK, total JNK, and actin were detected by Western blot using polyclonal (to phosphorylated and total JNK) and monoclonal antibodies (to actin).

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