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

Helen R. Griffiths, Joseph Lunec

Research output: Contribution to journalArticle

Abstract

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.
Original languageEnglish
Pages (from-to)161-164
Number of pages4
JournalFEBS Letters
Volume388
Issue number2-3
DOIs
Publication statusPublished - 17 Jun 1996

Fingerprint

Reactive Oxygen Species
Rheumatoid Arthritis
Immunoglobulin G
Hypochlorous Acid
In Vitro Techniques
Denaturation
Synovial Fluid
Polymorphism
Neutrophils
Enzyme-Linked Immunosorbent Assay
Fluids
Serum

Keywords

  • IgG
  • reactive oxygen species
  • C1q binding activity
  • rheumatoid arthritis

Cite this

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The C1q binding activity of IgG is modified in vitro by reactive oxygen species: implications for rheumatoid arthritis. / Griffiths, Helen R.; Lunec, Joseph.

In: FEBS Letters, Vol. 388, No. 2-3, 17.06.1996, p. 161-164.

Research output: Contribution to journalArticle

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