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Analysis of cyclin-dependent kinase 2-regulated phosphorylation of stathmin in etoposide-induced apoptotic HeLa cells by two-dimensional electrophoresis and mass spectrometry

Title
Analysis of cyclin-dependent kinase 2-regulated phosphorylation of stathmin in etoposide-induced apoptotic HeLa cells by two-dimensional electrophoresis and mass spectrometry
Author
임형신
Keywords
stathmin; cyclin-dependent kinase 2; cancer cell; etoposide; proteomic analysis
Issue Date
2005-04
Publisher
PHARMACEUTICAL SOC JAPAN
Citation
JOURNAL OF HEALTH SCIENCE, v. 51, No. 2, Page. 224-232
Abstract
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.
URI
https://www.jstage.jst.go.jp/article/jhs/51/2/51_2_224/_article/-char/ja/http://repository.hanyang.ac.kr/handle/20.500.11754/110222
ISSN
1344-9702; 1347-5207
DOI
10.1248/jhs.51.224
Appears in Collections:
COLLEGE OF PHARMACY[E](약학대학) > PHARMACY(약학과) > Articles
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