Proteins released from stimulated neutrophils contain very high levels of oxidized methionine

FEBS Letters

Beck-Speier, I.¹  Luippold, G.¹  Leuschel, L.¹  Maier, K.L.¹ 

[1] Projekt Inhalation der Gesellschaft für Strahlen- und Umweltforschung München, Arbeitsgruppe Biochemie, Ingolstädter Landstrasse 1, D-8042 Neuherberg, FRG 17111987

关键词: Extracellular oxidation;    Methionine;    Methionine sulfoxide;    Myeloperoxidase;    Neutrophil;    Met;    methionine;    Met(O);    methionine sulfoxide;    PMA;    phorbol myristate acetate;   

DOI  :  10.1016/0014-5793(88)81401-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown