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Glycogen synthase kinase-3beta regulates etoposide-induced apoptosis via Bcl-2 mediated caspase-3 activation in C3H10T1/2 cells.

Authors
Yun, SI; Yoon, HY; Chung, YS
Citation
Apoptosis : an international journal on programmed cell death, 14(6):771-777, 2009
Journal Title
Apoptosis : an international journal on programmed cell death
ISSN
1360-81851573-675X
Abstract
Glycogen synthase kinase-3beta (GSK3beta) controls the survival of osteoblasts during bone development through Wnt canonical signaling. GSK3beta is a key factor for osteoblastogenesis, but relatively less is known regarding its role in osteoblast apoptosis. Genotoxic stress induced by etoposide promoted apoptotic signaling by GSK3beta activation in C3H10T1/2 cells, a mouse mesenchymal cell line. Etoposide led to the time-dependent activation of GSK3beta and caspase-3, which resulted in PARP cleavage. LiCl (a specific inhibitor) and siRNA (gene knock-down) of GSK3beta prevented the effects of etoposide on apoptosis. Staurosporine also induced apoptosis in C3H10T1/2 cells, but LiCl could not rescue. Bcl-2 was decreased in the cells by exposure to etoposide. LiCl completely recovered Bcl-2 expression as shown by both the mRNA and the protein expression levels. In conclusion, etoposide-induced apoptosis in C3H10T1/2 cells is mediated by GSK3beta, which leads to caspase-3 activation via decrease in Bcl-2 expression.
MeSH terms
AnimalsApoptosis/drug effects*Caspase 3/metabolism*Cell LineCytoprotection/drug effectsEnzyme Activation/drug effectsEtoposide/pharmacology*Gene Expression Regulation, Enzymologic/drug effectsGene Silencing/drug effectsGlycogen Synthase Kinase 3/geneticsGlycogen Synthase Kinase 3/metabolism*Lithium Chloride/pharmacologyMiceProto-Oncogene Proteins c-bcl-2/metabolism*Staurosporine/pharmacology
DOI
10.1007/s10495-009-0348-4
PMID
19408126
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Endocrinology & Metabolism
AJOU Authors
정윤석
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