C1 inhibitor-dependent dissociation of human complement component C1 bound to immune complexes.
The interaction of C1 inhibitor with complement component C1 bound to immune complexes was examined by using 125I-labelled C1 subcomponents. The inhibitor binds rapidly to subcomponent C1s, and more slowly to subcomponent C1r. Formation of the C1r-C1 inhibitor complex causes rapid dissociation of subcomponents C1r and C1s from the antibody-antigen-component C1 aggregate. The rate and extent of this release are proportional to C1 Inhibitor concentration and are also dependent on ionic strength. Results obtained with purified C1 Inhibitor, plasma or serum as source of C1 Inhibitor are all closely comparable. Only slight dissociation of subcomponent C1q is observed under the same range of conditions. The implications of the release phenomenon are discussed in relation to the structure of component C1 and the possibility of differential turnover of C1 subcomponents.
D000915:Antibody Affinity; D000936:Antigen-Antibody Complex; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003172:Complement C1 / Q000276:immunology*; D003174:Complement C1 Inactivator Proteins / Q000276:immunology*; D006801:Humans; D046911:Macromolecular Substances; D009994:Osmolar Concentration
D000936:Antigen-Antibody Complex; D003172:Complement C1; D003174:Complement C1 Inactivator Proteins; D046911:Macromolecular Substances