Binding of serum immunoglobulins to collagens in IgA nephropathy and HIV infection.

Abstract:

:The mechanism of the binding of IgA to the mesangium in IgA nephropathy (IgAN) is unknown. Interactions between IgA and components of the mesangial matrix may contribute. We measured by enzyme-linked immunosorbent assay the binding of serum IgA, IgG, and IgM from patients with IgAN, human immunodeficiency virus type I (HIV) infection, and healthy controls to purified native collagen types I to VI, and to an extract of normal kidney tissue. HIV infection is an appropriate disease control because of the lack of mesangial IgA deposits, despite high serum levels of IgA and IgA1-containing immune complexes. Increased levels of IgA-binding to collagen types I and V and the kidney extract were found only in IgAN. Both IgAN and HIV-infected patients had increased IgA-binding to collagen types II, III, and VI. Preabsorption of the sera with gelatin substantially reduced the IgA-binding to collagen types I to IV, but not to types V and VI. This finding suggests that the binding to collagen type V is not fibronectin-mediated, but may reflect autoantibody formation. Thus, fibronectin-mediated IgA-collagen interactions are not specific for IgAN, and their pathogenetic role is questionable. The role of IgA anti-collagen type V antibodies requires further study.

journal_name

Kidney Int

journal_title

Kidney international

authors

van den Wall Bake AW,Kirk KA,Gay RE,Switalski LM,Julian BA,Jackson S,Gay S,Mestecky J

doi

10.1038/ki.1992.298

subject

Has Abstract

pub_date

1992-08-01 00:00:00

pages

374-82

issue

2

eissn

0085-2538

issn

1523-1755

pii

S0085-2538(15)57727-2

journal_volume

42

pub_type

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