Calcium overload is essential for the acceleration of staurosporine-induced cell death following neuronal differentiation in PC12 cells.
10.3858/emm.2009.41.4.030
- Author:
Su Ryeon SEO
1
;
Jeong Taeg SEO
Author Information
1. Department of Molecular Bioscience, School of Bioscience and Biotechnology, Kangwon National University, Chuncheon, Korea. suryeonseo@kangwon.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
bcl-X protein;
calcium;
cell death;
cell differentiation;
PC12 cells;
staurosporine
- MeSH:
Animals;
Calcium/*metabolism;
Caspase 3/metabolism;
Cell Differentiation/*physiology;
DNA Fragmentation;
Mitochondria/metabolism;
*Neurons/cytology/drug effects/physiology;
*PC12 Cells/cytology/drug effects/physiology;
Rats;
Staurosporine/*pharmacology;
bcl-X Protein/metabolism
- From:Experimental & Molecular Medicine
2009;41(4):269-276
- CountryRepublic of Korea
- Language:English
-
Abstract:
Differentiation of neuronal cells has been shown to accelerate stress-induced cell death, but the underlying mechanisms are not completely understood. Here, we find that early and sustained increase in cytosolic ([Ca2+]c) and mitochondrial Ca2+ levels ([Ca2+]m) is essential for the increased sensitivity to staurosporine-induced cell death following neuronal differentiation in PC12 cells. Consistently, pretreatment of differentiated PC12 cells with the intracellular Ca2+-chelator EGTA-AM diminished staurosporine-induced PARP cleavage and cell death. Furthermore, Ca2+ overload and enhanced vulnerability to staurosporine in differentiated cells were prevented by Bcl-XL overexpression. Our data reveal a new regulatory role for differentiation-dependent alteration of Ca2+ signaling in cell death in response to staurosporine.
