Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1937644 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
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.
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Authors
Hiroshi Ohno, Koichi Uemura, Kaori Shintani-Ishida, Mihoko Nakamura, Mitsushi Inomata, Ken-ichi Yoshida,