The Pathogenicity of Anti- XXXX -IgG Autoantibodies Depends on Fc Glycosylation.

@entity1 @entity32 @entity3172 @entity6300 @entity9500 @entity1701 @entity12009
UNASSIGNED: To analyze the glycosylation of anti- @entity9500 , we investigated purified IgG from healthy @entity1 , @entity1 with @entity12009 , and asymptomatic adult carriers of antiphospholipid antibodies. We observed that in the sera of healthy @entity1 and of @entity1 with @entity12009 , @entity3172 and IgG2 were predominant, respectively. The potentially protective anti- @entity9500 -IgM was lower in the sera of healthy children. Although anti- @entity9500 -associated @entity6300 did not differ between @entity1 and patients with @entity1701 , the associated C3c was significantly higher in the sera of healthy @entity1 . This indicates a more efficient clearance of anti- @entity9500 immune complexes in the healthy @entity1 . This clearance is not accompanied by @entity32 or coagulatory events. It is likely that the most important pathogenic factor of the anti- @entity9500 -IgG is related to the different glycosylation observed in healthy and diseased individuals. We detected a significantly higher sialylation of anti- @entity9500 -IgG isolated from the sera of healthy @entity1 and asymptomatic adults when compared with that of @entity1 with clinically apparent @entity1701 . Low sialylated IgG reportedly ameliorates @entity32 and @entity32 promotes hyposialylation. Thus, both reactions create a vicious circle that precipitates the pathology of the @entity1701 including thrombus-formation. We conclude that the increased sialylation of anti- @entity9500 -IgG of sera of healthy individuals limits their pathogenicity.
