Selective nuclear transport of mu-calpain.
Selective nuclear transport of mu-calpain.
复制标题
mu-钙蛋白酶的选择性核运输。
DOI：
10.1006/bbrc.1994.2493
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发表时间：
1994
影响因子：
3.1
通讯作者：
Lu,Q
中科院分区：
文献类型：
--
作者：
Mellgren,RL;Lu,Q
为了研究纯化的钙蛋白酶在体外系统中的核转运，用毛地黄皂苷透化A431细胞，并在已知促进蛋白质的能量依赖性核转运的条件下引入荧光素标记的钙蛋白酶。荧光素-μ-钙蛋白酶以ATP依赖的方式进入细胞核。calpain特异性抑制蛋白calpastatin不能阻断μ-calpain转位。荧光素-钙蛋白酶抑制素和荧光素-m-钙蛋白酶转运最好。在大鼠肝胞质因子存在下，约1 μM Ca 2+时细胞核μ-calpain的蓄积最大，0.3 μM Ca 2+时未观察到转运。大鼠红细胞和HeLa细胞提取物支持运输的Ca 2+的情况下。
To study nuclear transport of purified calpains in anin vitrosystem, A431 cells were permeabilized with digitonin, and fluorescein-labeled calpains were introduced under conditions known to facilitate energy-dependent nuclear transport of proteins. Fluorescein-μ-calpain was transported into nuclei in an ATP-dependent fashion. The calpain-specific inhibitor protein, calpastatin, could not block μ-calpain translocation. Fluorescein-calpastatin and fluorescein-m-calpain were poorly transported at best. In the presence of rat liver cytosolic factors accumulation of nuclear μ-calpain was maximum at approximately 1 μM Ca2+, and no transport was observed at 0.3 μM Ca2+. Rat erythrocyte and HeLa cell extracts supported transport in the absence of Ca2+.