RA-VII, a cyclic depsipeptide, changes the conformational structure of actin to cause G2 arrest by the inhibition of cytokinesis
RA-VII, a cyclic depsipeptide, changes the conformational structure of actin to cause G2 arrest by the inhibition of cytokinesis
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DOI：
10.1016/j.canlet.2003.12.022
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发表时间：
2004-06-25
期刊：
影响因子：
9.7
通讯作者：
Ohizumi, Y
中科院分区：
文献类型：
--
作者：
Fujiwara, H;Saito, S;Ohizumi, Y
在L12 - 10细胞中，RA-VII（0.1-100 nM）引起浓度依赖性的增殖抑制和G（2）阻滞。用10 nM RA-VII处理PCl 2细胞改变细胞形状，使细胞变圆，出现双核，表明胞质分裂受到抑制。与F-肌动蛋白结合的FITC-鬼笔环肽的荧光强度被RA-VII增强。在表面等离子体共振实验中，F-肌动蛋白的信号被RA-VII修饰，与结合到F-肌动蛋白的FITC-鬼笔环肽的浓度密切一致。这些结果表明，RA-VII引起F-肌动蛋白的构象变化和肌动蛋白丝的稳定，从而诱导G（2）阻滞。(C)2004爱思唯尔有限公司保留所有权利。
In L 12 10 cells, RA-VII (0.1-100 nM) caused the concentration-dependent inhibition of the proliferation and G(2) arrest. Treatment of PCl2 cells with 10 nM RA-VII changed cell shape round with binucleation, suggesting the inhibition of cytokinesis. The fluorescence intensity of FITC-phalloidin bound to F-actin was enhanced by RA-VII. In surface plasmon resonance experiments, the signal of F-actin was modified by RA-VII in close agreement with a concentration of FITC-phalloidin binding to F-actin. These results suggest that RA-VII causes the conformational change of F-actin and the stabilization of actin filaments to induce G(2) arrest. (C) 2004 Elsevier Ltd. All rights reserved.