INACTIVATION OF INTERLEUKIN-8 BY AMINOPEPTIDASE-N (CD13)
INACTIVATION OF INTERLEUKIN-8 BY AMINOPEPTIDASE-N (CD13)
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DOI：
10.1002/jlb.57.1.129
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发表时间：
1995-01-01
影响因子：
5.5
通讯作者：
TERAO, T
中科院分区：
文献类型：
--
作者：
KANAYAMA, N;KAJIWARA, Y;TERAO, T
氨基肽酶（APN）可降解白细胞介素-8 （IL-8）并使其趋化活性失活。白细胞介素-8的趋化活性被APN或中性粒细胞质膜剂量和时间依赖性地降低。在bestatin或WM15单克隆抗体存在下，趋化活性不灭活。流式细胞术检测IL-8的表达。在脂多糖（LPS）刺激下，IL-8的表达在60分钟内先升高后显著降低。相比之下，在LPS和bestatin处理下，IL-8的表达持续增加至少120分钟。这些结果表明，吞噬细胞中IL-8的表达和释放受APN对IL-8的蛋白水解作用的调控。
Aminopeptidase (APN) was found to degrade interleukin-8 (IL-8) and inactivate its chemotactic activity. The chemotactic activity of IL-8 was decreased by APN or neutrophil plasma membranes dose- and time-dependently. The chemotactic activity was not inactivated in the presence of bestatin or WM15 monoclonal antibody. The expression of IL-8 was measured by flow cytometry. On lipopolysaccharide (LPS) stimulation, IL-8 expression increased for 60 min and then decreased markedly. In contrast, on treatment with LPS and bestatin, the expression of IL-8 increased continuously for at least 120 min. These results suggest that the expression and release of IL-8 from phagocytic cells are regulated by the proteolytic effect of APN on IL-8.