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The C1q binding activity of IgG is modified in vitro by reactive oxygen species: implications for rheumatoid arthritis
Author(s) -
Griffiths H.R.,
Lunec J.
Publication year - 1996
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(96)00542-x
Subject(s) - chemistry , in vitro , hypochlorous acid , reactive oxygen species , rheumatoid arthritis , synovial fluid , complement system , immunoglobulin g , immunology , antibody , biochemistry , medicine , pathology , alternative medicine , osteoarthritis
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.