Vincristine regulates the phosphorylation of the antiapoptotic protein HSP27 in breast cancer cells
Vincristine regulates the phosphorylation of the antiapoptotic protein HSP27 in breast cancer cells
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DOI：
10.1016/j.canlet.2006.05.005
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发表时间：
2007-03-18
期刊：
影响因子：
9.7
通讯作者：
Ramos, Sofia
中科院分区：
文献类型：
--
作者：
Casado, Pedro;Zuazua-Villar, Pedro;Ramos, Sofia
长春新碱是一种抑制微管聚合、引起G2/M期阻滞和诱导细胞凋亡的抗肿瘤药物。2D-PAGE和MALDI-TOF-MS分析长春新碱对MCF7细胞的影响，揭示了长春新碱上调形式和长春新碱下调形式的抗凋亡蛋白HSP27。这些发现与长春新碱对HSP27mRNA缺乏影响有关，提示蛋白质翻译后修饰。进一步的分析表明，含有丝氨酸82的磷酸化肽只以长春新碱上调的形式存在。用特异性抗体证实丝氨酸82磷酸化。因此，HSP27的磷酸化可能在细胞对长春新碱的反应中发挥作用。(C)2006爱思唯尔爱尔兰有限公司。保留所有权利。
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.