51. Rheumatoid factor inhibition of in vitro binding of IgG complexes in the human glomerulus
- Author
-
Jon H. Schrock, John S. Davis, and W. Kline Bolton
- Subjects
biology ,Serial dilution ,Immunology ,Kidney Glomerulus ,Antigen-Antibody Complex ,In Vitro Techniques ,In vitro ,Guinea pig ,Immune system ,Rheumatology ,Biochemistry ,Immunoglobulin M ,In vivo ,Rheumatoid Factor ,Immunoglobulin G ,Complement C3b ,biology.protein ,Immunology and Allergy ,Rheumatoid factor ,Humans ,Pharmacology (medical) ,Bovine serum albumin ,Receptor - Abstract
We studied the effects of rheumatoid factor (RF) on binding of immune complexes to activated C3 (C3b) receptors in vitro. IgM fraction of serum containing RF activity (IgM-RF), IgM isolated from pooled normal human serum and having no RF activity (IgM-control), bovine serum albumin, and Veronal buffered saline solutions were used in a C3b assay system consisting of aggregated human IgG (AggHuIgG) coupled to sheep erythrocytes (SRBC) with guinea pig and normal human serum complement. The number of glomerular bound AggHuIgG-SRBC with IgM-control and bovine serum albumin or Veronal buffered saline was similar, while the number of bound cells with IgM-RF was reduced significantly. This effect was seen with both guinea pig and normal human serum complements. Supernatant hemolytic complement activity was maintained with IgM-RF, but reduced with control solutions. The blocking factor was shown to be RF by serial dilutions of IgM-RF resulting in inverse correlations with latex flocculation and inhibition of SRBC binding, absorption of blocking from IgM-RF with insolubilized AggHuIgG, and failure of IgM-control to block binding. IgM-RF did not directly interfere with activation of complement, but blocked attachment of C3 to AggHuIgG and formation of C3b capable of reacting with glomerular receptors. These results showed that IgM-RF can inhibit binding of AggHuIgG complexes to human glomeruli. This in vitro phenomenon may represent a possible protective mechanism of RF in vivo in diseases with immune complexes.
- Published
- 1982