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Characterization and synthesis of a macrophage inhibitory peptide from the second constant domain of human immunoglobulin G
Author(s) -
Auriault Claude,
Joseph Michel,
Tartar André,
Capron André
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80109-4
Subject(s) - chemistry , antibody , peptide , inhibitory postsynaptic potential , macrophage , constant (computer programming) , immunoglobulin g , characterization (materials science) , immunoglobulin domain , biochemistry , biology , in vitro , immunology , receptor , computer science , nanotechnology , neuroscience , materials science , programming language
We have shown that IgG hydrolysed by Schistosoma mansoni schistosomula inhibited various macrophage functions, especially phagocytosis and anti‐schistosome cytotoxicity. Here we show that a tripeptide, Thr 289 ‐Lys‐Pro 291 , 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 − 2 generation 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.