Vincristine regulates the phosphorylation of the antiapoptotic protein HSP27 in breast cancer cells

被引：35

作者：

Casado, Pedro ^{[1
]}

Zuazua-Villar, Pedro ^{[1
]}

del Valle, Eva ^{[1
]}

Martinez-Campa, Carlos ^{[1
]}

Lazo, Pedro S. ^{[1
]}

Ramos, Sofia ^{[1
]}

机构：

[1] Univ Oviedo, Dept Bioquim & Biol Mol, IUOPA, E-33071 Oviedo, Spain

来源：

CANCER LETTERS | 2007年 / 247卷 / 02期

关键词：

2D-PAGE; breast cancer; HSP27; MALDI-TOF-MS; phosphorylation; vincristine; CHINESE-HAMSTER CELLS; NECROSIS-FACTOR-ALPHA; HEAT-SHOCK-PROTEIN; PROTECTIVE ACTIVITY; ANTICANCER DRUGS; VINCA ALKALOIDS; CYTOCHROME-C; TUMOR-CELLS; RESISTANCE; APOPTOSIS;

D O I：

10.1016/j.canlet.2006.05.005

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Vincristine is an antitumor drug that inhibits microtubule polymerization, causes G2/M arrest and induces apoptosis. 2D-PAGE and MALDI-TOF-MS analysis of vincristine effects on MCF7 cells, revealed a vincristine upregulated form and a vincristine downregulated form of the antiapoptotic protein HSP27. These findings linked to the lack of vincristine effect over HSP27 mRNA, suggest a protein post-translational modification. Further assays indicated the presence of a phosphorylated peptide, containing serine 82, only in the vincristine upregulated form. Serine 82 phosporylation was confirmed using specific antibodies. Thus, phosphorylation of HSP27 may play a role in the cellular response to vincristine. (c) 2006 Elsevier Ireland Ltd. All rights reserved.

引用

页码：273 / 282

页数：10

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