Ischemia promotes calpain-mediated degradation of p120-catenin in SH-SY5Y cells

p120-Catenin contributes to the cadherin-mediated adhesion and aggregation of cells. μ-Calpain was activated and p120-catenin was degraded after 36 h of ischemia in differentiated SH-SY5Y cells. Calpain inhibitors Cbz-Val-Phe-H (MDL28170, 20 μM) and N-acetyl-leucyl-leucyl-norleucinal (ALLN, 20 μM) increased the levels of dephosphorylated p120-catenin, aggregation, and cell survival as detected by reduced LDH release in ischemic cells. However, a proteasome inhibitor lactacystin had no such effects. This is the first report of the calpain-mediated degradation of p120-catenin and an association between the level of dephosphorylated p120-catenin and cell aggregation in ischemic neuronal cells.