Publication: Methylation of histone H3 lysine 27 associated with apoptosis in osteosarcoma cells induced by staurosporine
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Date
2009
Authors
Cheng, Ming-Fang ; Lee, Chian-Her ; Hsia, Kan-Tai ; Huang, , Guo-Shu ; Lee, Herng-Sheng
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
The relationship between histone
methylation and apoptosis, programmed cell death, is
beginning to be explored. The objective of this study
was to investigate the effects of staurosporine, a PKC
inhibitor on the methylation of histone H3 in
osteosarcoma cells. Following stimulation by
staurosporine in vitro of G292 cells, a human
osteosarcoma cell line with fibroblast-like phenotype,
methylation of histone H3 was evaluated by western
blotting and immunocytochemistry. G292 cells revealed
the expression of cleaved PARP after incubation with
staurosporine for 3 hours. Monomethyl lysine (K) 27
was induced by staurosporine at a concentration of 1, but
no monomethyl K4 or K9 in histone H3 was seen.
Dimethyl and trimethyl histone H3 K27 were also
identified. There was no expression of dimethyl or
trimethyl histone H3 K4 and K9. Expression of
monomethyl histone H3 K27 was dose-dependent. The
morphologic changes of apoptosis induced by
staurosporine were observed under microscopy.
Immunocytochemistry of monomethyl histone H3 K27
showed a weak signal in controls, a strong signal in
staurosporine-treated tumor cells and a denser signal in
the apoptotic cells. Our studies demonstrated that
monomethyl histone H3 lysine 27 is expressed in
staurosporine-induced apoptotic osteosarcoma cells. The
findings may provide novel bridge information between
the epigenetic episodes and apoptotic process
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