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The Journal of Immunology, Vol 126, Issue 4 1387-1389, Copyright © 1981 by American Association of Immunologists

ARTICLES

Oxidation of n-formyl methionyl chemotactic peptide by human neutrophils

MF Tsan and RC Denison

Human neutrophils during phagocytosis oxidized the synthetic chemotactic peptide, n-formyl methionyl-leucyl-phenylalanine (n-FMLP), to its sulfoxide derivative (n-FMsLP). The oxidation of n-FMLP by phagocytosing neutrophils was inhibited by methionine, but not by methionine sulfoxide, leucine, or phenylalanine, confirming that it was the methionine moiety of n-FMLP that was oxidized. The oxidation of n- FMLP was also inhibited by myeloperoxidase inhibitors or catalase, but not by SOD or mannitol, suggesting the involvement of the myeloperoxidase system. Since n-FMsLP does not have chemotactic activity, the oxidation of n-FMLP by phagocytosing neutrophils may be one mechanism by which neutrophils modulate the inflammatory process.


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