Chelation of Extracellular Calcium-Induced Cell Death was Prevented by Glycogen Synthase Kinase-3 Inhibitors in PC12 Cells
| Autor: | Haruka Aoki, Megumi Ohtsuka, Tsuneo Takadera |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Programmed cell death
Indoles chemistry.chemical_element Apoptosis Calcium PC12 Cells Maleimides Glycogen Synthase Kinase 3 Cellular and Molecular Neuroscience chemistry.chemical_compound GSK-3 Nerve Growth Factor Extracellular Animals Insulin-Like Growth Factor I Glycogen synthase Egtazic Acid Heat-Shock Proteins Chelating Agents Cell Death biology Cell Biology General Medicine Benzazepines Molecular biology Rats Cell biology Enzyme Activation EGTA chemistry Caspases Second messenger system biology.protein |
| Zdroj: | Cellular and Molecular Neurobiology. 30:193-198 |
| ISSN: | 1573-6830 0272-4340 |
| Popis: | Calcium ion is a secondary messenger that mediates a variety of physiological responses of neurons, including cell survival responses. To determine the role of calcium in regulating neuronal survival and death, we examined whether chelation of extracellular calcium with EGTA induces caspase-dependent apoptotic cell death and whether glycogen synthase kinase-3 is involved in EGTA-induced cell death in PC12 cells. EGTA increased apoptotic cell death with morphological changes characterized by cell shrinkage and nuclear condensation and fragmentation accompanied by caspase activation. EGTA increased GRP78 protein expression, suggesting that EGTA induces ER stress. Glycogen synthase kinase-3 inhibitors prevented EGTA-induced apoptosis. In addition, nerve growth factor and insulin growth factor-I completely blocked EGTA-induced cell death. Moreover, caspase-3 activation was inhibited by glycogen synthase kinase-3 inhibitors. These results suggest that chelation of extracellular calcium with EGTA induces caspase-dependent apoptosis, and the activation of glycogen synthase kinase-3 is involved in the death of PC12 cells. |
| Databáze: | OpenAIRE |
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