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

Abstract

p120-catenin contributes to the cadherin-mediated adhesion and aggregation of cells. mu-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 microM) and N-acetyl-leucyl-leucyl-norleucinal (ALLN, 20 microM) 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.

• Authors: Hiroshi Ohno, Koichi Uemura, Kaori Shintani-Ishida, Mihoko Nakamura, Mitsushi Inomata, Ken-ichi Yoshida
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 353 Issue 3 Pg. 547-52 (Feb 16 2007) ISSN: 0006-291X [Print] United States
• PMID: 17196166 (Publication Type: Journal Article)

Chemical References

• Catenins
• Cell Adhesion Molecules
• Dipeptides
• Leupeptins
• Phosphoproteins
• acetylleucyl-leucyl-norleucinal
• lactacystin
• Calpain
• calpain inhibitor III
• Acetylcysteine
• Delta Catenin
• CTNND1 protein, human

Topics

• Acetylcysteine (analogs & derivatives, pharmacology)
• Calpain (antagonists & inhibitors, metabolism)
• Catenins
• Cell Adhesion Molecules (metabolism)
• Cell Aggregation (drug effects)
• Cell Death (drug effects)
• Cell Line, Tumor
• Dipeptides (pharmacology)
• Humans
• Ischemia (physiopathology)
• Leupeptins (pharmacology)
• Neuroblastoma (metabolism)
• Phosphoproteins (metabolism)
• Delta Catenin