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J.Health Sci., 51(2), 224-232, 2005
Analysis of Cyclin-Dependent Kinase 2-Regulated
Phosphorylation of Stathmin in Etoposide-Induced Apoptotic HeLa Cells by Two-Dimensional Electrophoresis and Mass Spectrometry
Yong-ung Kim, Kyo-Tan Koo, Joon-Seok Choi, Ying-Hua Jin, Hyungshin Yim, You-Take Oh, and Seung Ki Lee*
College of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, San 56-1, Sillim-dong,
Gwanak-gu, Seoul 151-742, Republic of Korea
The candidate proteins that are involved in the
cyclin-dependent kinase 2 (cdk2) signaling pathway
were analyzed by comparing different proteins between dominant negative cdk2 overexpressed and
control HeLa cells using two-dimensional electrophoresis
(2-DE) and mass spectrometry (MS). The 2-DE and MS indicated that stathmin and its
monophosphorylated form were induced in etoposide-treated HeLa
cells compared to untreated cells and this effect was
inhibited by overexpression of dominant negative mutant form of cdk2. Further analysis showed that
serine-25 (Ser-25), which comprises the conserved
target motif for phosphorylation by mitogen-activated
protein kinase (MAPK), was the major
phosphorylation site of monophosphorylated form of stathmin.
These findings indicate that etoposide-induced
expression and phosphorylation at Ser-25 of stathmin might
be mediated by activation of the MAPK signaling
pathway, which is mediated by the cdk2 activation during
the onset of the anticancer agent induced apoptotic
events in the cancer cells.
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