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Phosphorylation of beta-actin by protein kinase C-delta in camptothecin analog-induced leukemic cell apoptosis

, : Phosphorylation of beta-actin by protein kinase C-delta in camptothecin analog-induced leukemic cell apoptosis. Acta Pharmacologica Sinica 29(1): 135-142

This study was conducted to reveal new proteins involved in acute myeloid leukemia (AML) cell apoptosis. Using camptothecin analog NSC606985- induced leukemic U937 cell apoptosis as a model, this study performed a differential proteomic analysis during apoptosis induction. The significantly modulated protein was underwent further investigation in the apoptotic process. We found that beta-actin protein presented two different spots on the two-dimensional electrophoresis (2-DE) map, which shared similar molecular weight and different pI. Those two spots demonstrated contrary changes (disappeared on the basic-end and increased on the acid-end spot) during apoptosis induction, although the total level of beta-actin kept constant. This observation was further confirmed by immunoblot analysis on 2-DE gel. When NSC606985-treated cell lysate was incubated with alkaline phosphotase, beta-actin on the basic-end spot was restored, indicating increased phosphorylation of beta-actin during NSC606985- induced apoptosis. Moreover, the polymerization of actin also decreased after NSC606985 treatment. The increased beta-actin phosphorylation and decreased actin polymerization was antagonized by pre-treatment of rottlerin, a specific protein kinase C-delta (PKC delta) inhibitor. All these results indicate that beta-actin was phosphorylated during apoptosis induction, which was mediated by activated PKC delta.


PMID: 18158875

DOI: 10.1111/j.1745-7254.2008.00753.x

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