CHARACTERIZATION AND SYNTHESIS OF A MACROPHAGE INHIBITORY PEPTIDE FROM THE 2ND CONSTANT DOMAIN OF HUMAN IMMUNOGLOBULIN-G
CHARACTERIZATION AND SYNTHESIS OF A MACROPHAGE INHIBITORY PEPTIDE FROM THE 2ND CONSTANT DOMAIN OF HUMAN IMMUNOGLOBULIN-G
复制标题
DOI：
10.1016/0014-5793(83)80109-4
复制
发表时间：
1983-01-01
期刊：
影响因子：
3.5
通讯作者：
CAPRON, A
中科院分区：
文献类型：
--
作者：
AURIAULT, C;JOSEPH, M;CAPRON, A
我们已经证明，由曼氏血吸虫水解的IgG可以抑制巨噬细胞的各种功能，特别是吞噬和抗血吸虫细胞毒性。在这里，我们展示了人类免疫球蛋白G（肽286-292）的第二个恒定结构域的三肽Thr289‐Lys‐Pro291再现了全水解产物的抑制作用。事实上，在预先用Thr - Lys - Pro （500 nmol/ml）孵育后，IgE -抗IgE -刺激的大鼠和人巨噬细胞释放的β -葡萄糖醛酸酶减少，细胞内水平没有上升。此外，三肽可减少细胞迁移和超氧阴离子O - 2生成50-80%。这些结果表明，在哺乳动物宿主寄生虫感染的早期阶段，单一肽组可能导致巨噬细胞功能下降。这种三肽的药理学性质正在研究中。
We have shown that IgG hydrolysed bySchistosoma mansonischistosomula inhibited various macrophage functions, especially phagocytosis and anti‐schistosome cytotoxicity. Here we show that a tripeptide, Thr289‐Lys‐Pro291, of the second constant domain of human immunoglobulin G (peptide 286–292) reproduced the inhibitory effect of a total hydrolysate. Indeed the β‐glucuronidase release from IgE‐anti‐IgE‐stimulated rat and human macrophages decreased and its intracellular level did not rise after a prior incubation of the cells with Thr‐Lys‐Pro (500 nmol/ml). Moreover, the cell migration as well as the superoxide anion O−2generation were 50–80% reduced by the tripeptide. These results suggest that a single peptide set may be responsible for the decrease of the macrophage functions at the early stage of the parasite infection in the mammalian host. The pharmacologic properties of this tripeptide are under investigation.