PROTEINS RELEASED FROM STIMULATED NEUTROPHILS CONTAIN VERY HIGH-LEVELS OF OXIDIZED METHIONINE
PROTEINS RELEASED FROM STIMULATED NEUTROPHILS CONTAIN VERY HIGH-LEVELS OF OXIDIZED METHIONINE
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DOI：
10.1016/0014-5793(88)81401-7
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发表时间：
1988-01-18
期刊：
影响因子：
3.5
通讯作者：
MAIER, KL
中科院分区：
文献类型：
--
作者：
BECKSPEIER, I;LEUSCHEL, L;MAIER, KL
在孵育期间从静止的人类中性粒细胞释放的蛋白质中，发现 21% 的蛋氨酸 (Met) 残基被氧化。然而，用酵母聚糖刺激细胞后，细胞外蛋白质中氧化的 Met 部分增加至 66%，用佛波醇肉豆蔻酸酯乙酸酯 (PMA) 刺激后，增加至 75%。迄今为止，尚未观察到活化的中性粒细胞在天然蛋白质中产生如此高水平的氧化蛋氨酸。在 PMA 刺激的细胞孵育过程中，超氧化物歧化酶的存在对蛋氨酸氧化产生的影响可以忽略不计，而过氧化氢酶的存在则导致释放的蛋白质中蛋氨酸磺氧化物 (Met(O)) 含量仅为 28%。据推测，这些蛋白质中的 Met 转化为 Met(O) 主要是通过细胞外空间中的髓过氧化物酶/H2O2/Cl−系统的作用发生的。
In proteins released from quiescent human neutrophils during incubation, 21% of the methionine (Met) residues were found to be oxidized. However, the portion of oxidized Met in extracellular proteins increased to 66% after stimulating the cells with zymosan and to 75% after stimulation with phorbol myristate acetate (PMA). Generation of such high levels of oxidized Met in native proteins by activated neutrophils has, so far, not been observed. The presence of superoxide dismutase during incubation of PMA‐stimulated cells produced a negligible effect on methionine oxidation, while the presence of catalase resulted in a methionine suifoxide (Met(O)) content of only 28% in the released proteins. It is proposed that the conversion of Met to Met(O) in these proteins predominantly occurs by action of the myeloperoxidase/ H2O2/Cl−system in the extracellular space.