Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 148-156 |
| Number of pages | 9 |
| Journal | Scandinavian Journal of Rheumatology |
| Volume | 17 |
| Issue number | s75 |
| DOIs | |
| Publication status | Published - 1988 |
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Keywords
- Immunoglobulin
- rheumatoid patient
- autoantibody
- oxygen radical
- polymorph
- polyclonal rheumatoid factors
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}
Effect of polymorph derived oxidants on IgG in relation to rheumatoid factor binding. / Griffiths, Helen R.; Lunec, Joseph.
In: Scandinavian Journal of Rheumatology, Vol. 17, No. s75, 1988, p. 148-156.Research output: Contribution to journal › Article
TY - JOUR
T1 - Effect of polymorph derived oxidants on IgG in relation to rheumatoid factor binding
AU - Griffiths, Helen R.
AU - Lunec, Joseph
PY - 1988
Y1 - 1988
N2 - Immunoglobulin G from rheumatoid patients is denatured around the hinge region. This has been proposed as an explanation for the presence of circulating autoantibodies to IgG in these patients. It has previously been suggested that oxygen radicals (OR) derived from activated polymorphs may play a role in denaturation in vivo. Using sera from rheumatoid patients and age-matched controls in a modified ELISA technique, we have investigated the potential for polyclonal rheumatoid factors (RF) to bind to OR denatured IgG. Three model systems were used to generate OR in vitro: (a) purified PMN s activated by the cell surface stimulant PMA, (b) radiolysis of IgG in solution to generate specifically the superoxide radical and, in a separate system, the hydroxyl radical, (OH.), (c) purified myeloperoxide in the presence of H2O2 and halide ions. Results: 1. The binding of both IgA and IgM RF s to PMN denatured IgG increased dose dependently for seropositive sera only. 2. The OH. radical but not the superoxide radical significantly increased the binding of IgA and M RF, again only for seropositive sera. 3. The myeloperoxidase enzyme system did not increase RF binding. 4. IgG incubated with elastase was not found to be a better antigen than native IgG. These results indicate that IgG is denatured by OR released from activated PMN, thereby producing an antigen for polyclonal RF s.
AB - Immunoglobulin G from rheumatoid patients is denatured around the hinge region. This has been proposed as an explanation for the presence of circulating autoantibodies to IgG in these patients. It has previously been suggested that oxygen radicals (OR) derived from activated polymorphs may play a role in denaturation in vivo. Using sera from rheumatoid patients and age-matched controls in a modified ELISA technique, we have investigated the potential for polyclonal rheumatoid factors (RF) to bind to OR denatured IgG. Three model systems were used to generate OR in vitro: (a) purified PMN s activated by the cell surface stimulant PMA, (b) radiolysis of IgG in solution to generate specifically the superoxide radical and, in a separate system, the hydroxyl radical, (OH.), (c) purified myeloperoxide in the presence of H2O2 and halide ions. Results: 1. The binding of both IgA and IgM RF s to PMN denatured IgG increased dose dependently for seropositive sera only. 2. The OH. radical but not the superoxide radical significantly increased the binding of IgA and M RF, again only for seropositive sera. 3. The myeloperoxidase enzyme system did not increase RF binding. 4. IgG incubated with elastase was not found to be a better antigen than native IgG. These results indicate that IgG is denatured by OR released from activated PMN, thereby producing an antigen for polyclonal RF s.
KW - Immunoglobulin
KW - rheumatoid patient
KW - autoantibody
KW - oxygen radical
KW - polymorph
KW - polyclonal rheumatoid factors
UR - https://www.tandfonline.com/doi/abs/10.3109/03009748809096756
U2 - 10.3109/03009748809096756
DO - 10.3109/03009748809096756
M3 - Article
VL - 17
SP - 148
EP - 156
JO - Scandinavian Journal of Rheumatology
JF - Scandinavian Journal of Rheumatology
SN - 0301-3847
IS - s75
ER -