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Interaction between fibronectin, rheumatoid factor and aggregated gamma globulins
The Journal of Rheumatology
|August 1, 1985
Summary
Fibronectin (Fn) was found in rheumatoid factor (RF) positive serum, suggesting it interacts with IgM RF and aggregated IgG. This interaction occurs in the Fc fragment, distinct from protein A and complement binding sites.
Area of Science:
- Immunology
- Biochemistry
Background:
- Rheumatoid factor (RF) is associated with rheumatoid arthritis.
- Fibronectin (Fn) is a protein found in serum and extracellular matrix.
Purpose of the Study:
- To investigate the interaction between fibronectin (Fn) and rheumatoid factor (RF).
- To determine if Fn binds to IgM RF and heat-aggregated human IgG.
Main Methods:
- Detection of Fn in polyethylene glycol precipitates of RF-positive serum.
- Assays to test the binding capacity of Fn with IgM RF and aggregated IgG.
Main Results:
- Fibronectin (Fn) was detected in 12 out of 14 RF-positive serum samples.
- Data suggest Fn directly interacts with both IgM RF and heat-aggregated human IgG.
- The binding site appears to be within the Fc fragment of immunoglobulins, distinct from protein A and complement binding sites.
Conclusions:
- Fibronectin (Fn) may play a role in the immune response in rheumatoid arthritis.
- Fn's interaction with immunoglobulins could be significant in RF-associated conditions.
- Further research is needed to pinpoint the exact binding site on the immunoglobulin Fc fragment.