The C1q binding activity of IgG is modified in vitro by reactive oxygen species: implications for rheumatoid arthritis

FEBS Letters

Lunec, J.¹  Griffiths, H.R.¹ 

[1] Division of Chemical Pathology, Hodgkin Building, P.O. Box 138, Leicester LE1 9HN, UK

关键词: IgG;    Reactive oxygen species;    C1q binding activity;    Rheumatoid arthritis;   

DOI  :  10.1016/0014-5793(96)00542-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

IgG can be denatured in vitro by reactive oxygen species (ROS). Native IgG activates the complement cascade through C1q. Using a modified ELISA, C1q binding activity of rheumatoid IgG has been compared to IgG denatured by neutrophil-derived ROS. The C1q binding activity of rheumatoid synovial fluid IgG is greater than the corresponding serum IgG (P < 0.01). Denaturation of IgG by activated polymorphs or the Fenton reaction decreased its C1q binding activity (P < 0.01). In vitro exposure of IgG to OH^· and ROO^· increased its interaction with C1q (P < 0.01). Hypochlorous acid had no effect. ROS-induced alteration to IgG-C1q binding activity may promote the inflammatory response in rheumatoid arthritis.

【 授权许可】

Unknown