Serum Immunoglobulins in Heymann's Experimental Nephritis Modulate Binding of Properdin and Factor-H to Sulpho-Glycosphingolipids II3SO3(-)-Gg3Cer and III3SO3(- )-, II3SO3( -GgsCer

• Published in: Journal of biochemistry (Tokyo) 1994-08, Vol.116 (2), p.450-456
• Main Authors: Jennemann, Richard, Schulze, Matthias, Bauer, Bernhard L., Kurtz, Christian, Wiegandt, Herbert
• Format: Article
• Language: English
• Subjects: alternative pathway of complement activation; complement factor-H; Heymann's nephritis; II3SO3( -)-Gg3Cer (Stril2; III3SO3(-); properdin; SB2; SM2; sulpho-glycosphingolipids II3SO3( - )-Gg3Cer (Stril1
• ISSN: 0021-924X
• DOI: 10.1093/oxfordjournals.jbchem.a124545

The nephropathic effects of Heymann's experimental nephrites involve autoallergic serum antibodies directed against rat kidney membrane constituents. In assessing the action of glycolipids as possible autoallergens in these conditions, it was found that heterologous and autologous Heymann's nephritis sera antibodies recognize the rat kidney sulphatides, II3SO3( - )-Gg3Cer (Stril), and III3SO3(-)-, II3SO3(-)-Gg3Cer (Stri2). Two antibody populations in Heymann's sera, each reacting with only one of the two sulphatides, could be observed. It was further shown that human factor-H and properdin, pivotal regulators of the alternative pathway of complement activation, both bound to Stri2 in vitro. This binding of factor-H and properdin was differentially affected by affinity-purified anti-Stri2 antibodies of Heymann's nephritis sera. Whereas the interaction between factor-H and Strj2 was inhibited by the antibody, that of properdin was enhanced.