Activation of the complement system by polysaccharidic surfaces bearing carboxymethyl, carboxymethylbenzyl-amide and carboxymethylbenzylamide sulphonate groups

Abstract

Substituted Sephadex ® derivatives bearing carboxymethyl (CM), CM-benzylamide (CMB), CM-propylamide (CMP) and CMB-sulphonate (CMBS) groups are used as models of polysaccharidic surfaces to measure the effects of substituting OH groups on the complement activating capacity (CAC) of the modified surfaces in normal human serum. CM substitution decreases and can suppress the CAC of Sephadex. Low CMB substitution also decreases the CAC, whereas high CMB or CMP substitutions increase it again after a minimum. In addition to C3 cleavage occurring at high substitution with CMB or CMP groups, the presence of CMB induces consumption of a protein, limiting CH50 measurements. The CAC variations could be due to rearrangements of the polymer surfaces at the aqueous interface with proteins. Highly substituted CMB-bearing surfaces could activate complement-like polystyrene surfaces. The presence of CMBS groups does not reduce the CAC of the surface. Such polymer surfaces, which are heparin-like concerning coagulation, are not heparin-like concerning complement inhibition.