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Differences in the Complement Activation Induced by Preformed and Nascent Immune Complexes

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While preformed BSA-anti-BSA immune complexes (PIC) bind efficiently to human RBC after their interaction with human complement, nascent BSA-anti-BSA immune complexes (NIC) formed in the presence of complement do not bind to autologous RBC. The same results were obtained with tetanus toxoid-anti-tetanus toxoid PIC and NIC. In order to elucidate the causes of this marked difference between the RBC-binding properties of PIC and NIC, the profile of complement activation induced by them was compared using haemolytic assays and sensitive ELISA tests. BSA-anti-BSA NIC activated Cl more efficiently than PIC. This was reflected in a higher C4 content of the isolated NIC and higher Cl INH-Cls and lower Clq-fibronectin complex level in the NIC-treated serum as compared to the PIC-treated ones. Although isolated NIC contained more C3 than isolated PIC did, there was no significant difference in the AP activation. These findings suggest that the failure of NIC to bind to RBC is not due to a lack of C4-binding, or C3-binding and/or activation, but rather to the special structure of this type of complex.
Title: Differences in the Complement Activation Induced by Preformed and Nascent Immune Complexes
Description:
While preformed BSA-anti-BSA immune complexes (PIC) bind efficiently to human RBC after their interaction with human complement, nascent BSA-anti-BSA immune complexes (NIC) formed in the presence of complement do not bind to autologous RBC.
The same results were obtained with tetanus toxoid-anti-tetanus toxoid PIC and NIC.
In order to elucidate the causes of this marked difference between the RBC-binding properties of PIC and NIC, the profile of complement activation induced by them was compared using haemolytic assays and sensitive ELISA tests.
BSA-anti-BSA NIC activated Cl more efficiently than PIC.
This was reflected in a higher C4 content of the isolated NIC and higher Cl INH-Cls and lower Clq-fibronectin complex level in the NIC-treated serum as compared to the PIC-treated ones.
Although isolated NIC contained more C3 than isolated PIC did, there was no significant difference in the AP activation.
These findings suggest that the failure of NIC to bind to RBC is not due to a lack of C4-binding, or C3-binding and/or activation, but rather to the special structure of this type of complex.

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