TLR4 decreases Wnt signaling at the level of the LRP6 receptor activation in Muller glia MIO-M1 cells.

<p>(A) Representative Western blots showing changes in phosphorylation status with Wnt signaling and LPS. Wnt3a conditioned media (W) increases the levels of phospho-Ser1490 LRP6 (p-LRP6) compared with control conditioned media (C). The addition of LPS reduces p-LRPS in Wnt3a treated cultures. In contrast, the amount of phospho-Ser9 in GSK3β is not affected by LPS. (B–C) Quantification of phospho-LRP6 and phospho-GSK3β. Twenty micrograms of total protein were loaded in each lane. The phosphorylated proteins were detected by phospho-specific antibodies and normalized to β-actin as a labeled control, and total LRP6 and GSK3β proteins were detected by antibodies that recognize both their respective phospho- and unphosphorylated forms, and normalized to β-actin. #, Wnt3a compared with control p<0.05, n = 5; *, Wnt3a compared with Wnt3a+LPS p<0.05, n = 5.