| 9485198 |
Druet E, Praddaude F, Druet P, Dietrich G: Non-immunoglobulin serum proteins prevent the binding of IgG from normal rats and from rats with Th2-mediated autoimmune glomerulonephritis to various autoantigens including glomerular antigens. Eur J Immunol. 1998 Jan;28(1):183-92.
It is now well established in normal humans and mice that purification of IgG from serum unmasks their autoantibody activity. Mercuric chloride (HgCl2) induces in Brown-Norway (BN) rats a Th2-dependent polyclonal B cell activation, a huge increase in serum IgE and IgG1 concentrations, the production of numerous autoantibodies and an autoantibody-mediated glomerulonephritis. In the present study we have compared the IgG autoantibody activity in the serum and in the purified IgG fraction from normal and HgCl2-injected BN rats. IgG autoantibodies were found to be masked in normal serum by non-immunoglobulin (nonIg) serum proteins and, provided these IgG did not encounter normal serum proteins, they could bind to glomerular antigens as assessed by immunofluorescence in a unilateral perfused kidney model. As a consequence of HgCl2-induced polyclonal activation of B cells, IgG autoantibodies were no longer complexed to non-Ig serum proteins, they were easily detected in the serum and could therefore reach their glomerular target. However, these autoantibodies could still be blocked by normal non-Ig serum proteins not only in vitro but also in a unilateral perfused kidney model so that their binding to glomerular antigens could be prevented. These findings indicate that the ratio between autoantibody level and the amount of non-Ig serum proteins may be crucial in autoantibody-mediated autoimmune diseases. |
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