TRANSIENT INCREASE IN VIMENTIN PHOSPHORYLATION AND VIMENTIN-HSC70 ASSOCIATION IN 9L RAT-BRAIN TUMOR-CELLS EXPERIENCING HEAT-SHOCK
TRANSIENT INCREASE IN VIMENTIN PHOSPHORYLATION AND VIMENTIN-HSC70 ASSOCIATION IN 9L RAT-BRAIN TUMOR-CELLS EXPERIENCING HEAT-SHOCK
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DOI：
10.1002/jcb.240540111
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发表时间：
1994-01-01
影响因子：
4
通讯作者：
LAI, YK
中科院分区：
文献类型：
--
作者：
CHENG, TJ;LAI, YK
在45℃处理的9L大鼠脑肿瘤细胞中，研究了波形蛋白的特征变化。在热休克处理过程中，波形蛋白分子被迅速磷酸化，并从丝状结构重组为核周高阶结构，非离子洗涤剂难以提取。研究发现，这些效应是高度短暂的，在热休克治疗开始后30分钟达到峰值，此后消退。同时，本构表达的热休克蛋白70 （HSC70）的溶解度也暂时降低，其动力学与波形蛋白相同。结果表明，HSC70与vimentin在热休克过程中共不溶。我们认为，由vimentin磷酸化增强引起的中间丝的重组导致HSC70与中间丝同时结合。这一过程可能在调节热休克基因中起重要作用。(C) 1994 Wiley-Liss, Inc。
Characteristic changes in vimentin were studied in 9L rat brain tumor cells treated at 45 degrees C. During heat-shock treatment, vimentin molecules were rapidly phosphorylated and reorganized from a filamentous form into a perinuclear higher-order structure that was less extractable by nonionic detergent. These effects were found to be highly transient, peaked at 30 min after the onset of heat-shock treatment, and subsided thereafter. Simultaneously, the solubility of the constitutively expressed heat-shock protein70 (HSC70) was also temporarily decreased and the kinetics was identical to that of vimentin. The results indicated that HSC70 and vimentin were co-insolubilized during the heat-shock treatment. We propose that the reorganization of the intermediate filaments resulted from enhanced phosphorylation of vimentin leads to the concurrent association of HSC70 to the intermediate filaments. This process may play an essential role in regulating heat-shock genes. (C) 1994 Wiley-Liss, Inc.