UBIQUITIN IS ASSOCIATED WITH AGGREGATES OF ARGININE MODIFIED PROTEINS IN INJURED NERVES
UBIQUITIN IS ASSOCIATED WITH AGGREGATES OF ARGININE MODIFIED PROTEINS IN INJURED NERVES
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DOI：
10.1097/00001756-199201000-00012
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发表时间：
1992-01-01
期刊：
影响因子：
1.7
通讯作者：
INGOGLIA, NA
中科院分区：
文献类型：
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作者：
JACK, DL;CHAKRABORTY, G;INGOGLIA, NA
大鼠坐骨神经的挤压损伤导致蛋白质翻译后酰基化增加10倍。在其他系统中，N-末端腺苷酸化导致腺苷酸化蛋白的泛素化和蛋白水解。在本实验中，用H-3-精氨酸对从150 kg压碎的坐骨神经上清液中获得的蛋白质进行后处理修饰。这些精氨酸修饰的蛋白质形成聚集体（在20 kg下沉淀），然后通过SDS-PAGE部分分离，其对泛素的单克隆抗体具有免疫反应性。结果表明，坐骨神经损伤后，某些蛋白质被泛素化和泛素化，可能靶向它们进行降解。很可能这些反应有助于清除细胞中被挤压破坏的蛋白质，否则这些蛋白质将具有细胞毒性。
CRUSH injury to rat sciatic nerves results in a 10-fold increase in the post-translational arginylation of proteins. In other systems, N-terminal arginylation leads to ubiquitination and proteolysis of the arginylated proteins. in the present experiments, proteins obtained from the 150 kg supernatant of crushed sciatic nerves were post-translationally modified by H-3-arginine. These arginine modified proteins formed aggregates (precipitated at 20 kg) which then partially separated by SDS-PAGE were immunoreactive to a monoclonal antibody to ubiquitin. The results indicate that following injury to sciatic nerves, certain proteins are arginylated and ubiquitinated, probably targeting them for degradation. It is likely that these reactions help to rid cells of proteins damaged by the crush which would otherwise be cytotoxic.