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艾氏腹水癌细胞中波形蛋白的周转

The turnover of vimentin in Ehrlich ascites tumour cells.

作者信息

McTavish C F, Nelson W J, Traub P

出版信息

FEBS Lett. 1983 Apr 18;154(2):251-6. doi: 10.1016/0014-5793(83)80159-8.

DOI:10.1016/0014-5793(83)80159-8
PMID:6299801
Abstract

The turnover of vimentin and vimentin-derived peptides has been examined in logarithmically growing Ehrlich ascites tumour cells. Cells were pulse-labelled with [35S]methionine for 30 min and then chased for up to 60 h. It was found that the specific radioactivity of the main isoelectric variant of vimentin decreased to half the original value in 15.3 h which was close to the division time of the cells (16 h). The protein moiety of the phosphorylated variant of vimentin also turned over very slowly, in contrast to the turnover rate of the phosphate group itself which has a half-life of 1.4 h. The role of the intermediate filament-specific, Ca2+-activated proteinase has been considered in relationship to the slow turnover of vimentin.

摘要

在对数生长期的艾氏腹水瘤细胞中检测了波形蛋白及其衍生肽段的周转情况。细胞用[35S]甲硫氨酸脉冲标记30分钟,然后追踪长达60小时。结果发现,波形蛋白主要等电变体的比放射性在15.3小时内降至原始值的一半,这与细胞的分裂时间(16小时)相近。波形蛋白磷酸化变体的蛋白质部分周转也非常缓慢,与之形成对比的是,磷酸基团本身的周转速率半衰期为1.4小时。已经探讨了中间丝特异性的、Ca2+激活的蛋白酶在波形蛋白缓慢周转方面的作用。

相似文献

1
The turnover of vimentin in Ehrlich ascites tumour cells.艾氏腹水癌细胞中波形蛋白的周转
FEBS Lett. 1983 Apr 18;154(2):251-6. doi: 10.1016/0014-5793(83)80159-8.
2
Efficient degradation in vitro of all intermediate filament subunit proteins by the Ca2+-activated neutral thiol proteinase from Ehrlich ascites tumor cells and porcine kidney.艾氏腹水瘤细胞和猪肾中钙激活中性硫醇蛋白酶对所有中间丝亚基蛋白的高效体外降解作用。
Biosci Rep. 1986 Jan;6(1):57-64. doi: 10.1007/BF01145179.
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Proteolysis of vimentin and desmin by the Ca2+-activated proteinase specific for these intermediate filament proteins.由对这些中间丝蛋白具有特异性的钙离子激活蛋白酶对波形蛋白和结蛋白进行蛋白水解。
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Large scale isolation, purification, and partial characterization of the intermediate filament-specific, Ca2+-activated proteinase from porcine kidney and Ehrlich ascites tumor cells: a comparative study.猪肾和艾氏腹水瘤细胞中中间丝特异性钙激活蛋白酶的大规模分离、纯化及部分特性分析:一项比较研究
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Probing of the structural stability of vimentin and desmin-type intermediate filaments with Ca2+-activated proteinase, thrombin and lysine-specific endoproteinase Lys-C.用钙离子激活蛋白酶、凝血酶和赖氨酸特异性内肽酶Lys-C探究波形蛋白和结蛋白型中间丝的结构稳定性
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Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments.波形蛋白N端多肽在中间丝形成中的作用。
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Properties of Ca2+-activated protease specific for the intermediate-sized filament protein vimentin in Ehrlich-ascites-tumour cells.艾氏腹水瘤细胞中对中间丝蛋白波形蛋白具有特异性的钙离子激活蛋白酶的特性
Eur J Biochem. 1981 May;116(1):51-7. doi: 10.1111/j.1432-1033.1981.tb05299.x.

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