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Complement-dependent binding of C-reactive protein complexes to human erythrocyte CR1
1Department of Microbiology, University of New Mexico, Albuquerque 87131, USA.
Clinical Immunology and Immunopathology
|November 1, 1996
Summary
C-reactive protein (CRP) complexes bind to complement receptors on erythrocytes. This suggests CRP complexes are cleared via the erythrocyte CR1 pathway, similar to immune complexes.
Area of Science:
- Immunology
- Biochemistry
- Complement System
Background:
- C-reactive protein (CRP) is an acute phase protein that binds to phosphocholine and chromatin components.
- CRP-ligand complexes activate complement and bind to phagocytic cell receptors.
- Complement is essential for clearing CRP-ligand coated erythrocytes, but its role in soluble CRP complex clearance is unknown.
Purpose of the Study:
- To investigate the role of complement and complement receptors in the clearance of soluble C-reactive protein (CRP) complexes.
- To determine if CRP-ligand complexes utilize the same clearance pathways as soluble immune complexes.
Main Methods:
- Prepared complexes using phosphocholine-conjugated BSA with either IgG antibody or CRP.
- Assessed complement-mediated binding of these complexes to human erythrocyte complement receptors (CR1, CD35).
- Utilized serum deficient in C4A or C4B to evaluate complement's role in complex binding.
Main Results:
- Both CRP and IgG complexes showed similar complement-mediated binding to erythrocyte CR1 (CD35).
- Serum deficient in C4A or C4B still supported the binding of CRP and IgG complexes to erythrocytes.
- These findings suggest a shared clearance mechanism for CRP and IgG complexes.
Conclusions:
- Soluble C-reactive protein (CRP) complexes can bind to erythrocyte complement receptor 1 (CR1).
- The CR1 pathway, previously described for soluble immune complexes, appears to mediate the clearance of CRP-ligand complexes.
- CRP complexes may be cleared from circulation via the erythrocyte CR1 pathway.