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C. Johansson, R. Butkowski, P. Swedenborg, P. Alm, J. Wieslander, Characterization of a non-Goodpasture autoantibody to type IV collagen, Nephrology Dialysis Transplantation, Volume 8, Issue 11, 1993, Pages 1205–1210, https://doi.org/10.1093/ndt/8.11.1205
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Abstract
Goodpasture's syndrome is a very severe and aggressive autoimmune kidney disease. The patients' autoantibodies, which are pathogenic, are restricted to the C-terminal region of the α3-chain of type IV collagen. In this paper we characterize an antitype IV collagen antibody from a patient with a nonprogressive form of glomerulonephntis.
ELISA and immunoblotting were used to study the specificity of this patient's antibodies. The patient had high titres of antibodies restricted to the C-terminal region of the αl-chain of type IV collagen. The antibody recognized an epitope hidden in the NC1 molecule which was fully exposed after denaturation or reduction. It was an IgG3 antibody composed of only lambda light chains, indicating that it has a potential to induce inflammatory damage and that it is probably monoclonal. This patient also had MPO-ANCA which were of IgGl subclass. Our patient had no disease progression during the 5 years of treatment.
Even though the anti-α1 (IV) antibodies react with the same domain, but of a different chain of type IV collagen compared to the Goodpasture's antibodies, they do not induce any severe damage. It is thus uncertain if the anti-α1 (IV) antibodies have any pathogenic role; the kidney damage might have been caused by the MPO-ANCA.
The findings support the theory that the anti-α3(IV) antibody causes disease in Goodpasture's syndrome and that antibodies restricted to other subunits of the C-terminal region of type IV collagen are less harmful.
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