Erythrocyte complement receptors.

Primate erythrocytes express complement receptors (E-CR), which can extrinsically bind C3b and Cb4. This interaction allows primate erythrocytes to bind complement opsonized particles and immune complexes, a phenomenon historically referred to as immune adherence. The binding of C3b and C4b by E-CR also leads to inhibition of complement activation. The human E-Cr is the complement activation. The human E-CR is the complement receptor type 1, or CR1, which is codominantly expressed as four polymorphic allotypes, ranging in size from 190,000 to 280,000 M(r). Non-human primate E-CR are similar to CR1 in function and antigenicity and are likely homologous to CR1 in structure; however, they are one third to one half the size of CR1. The physiological role of E-CR, determined from studies in monkeys and humans, is to allow erythrocytes to perform as inert shuttles for circulating immune complexes (IC), safely directing IC to the organs of the monocyte phagocytic system, thus preventing indiscriminate IC deposition in vulnerable tissue. In IC-mediated diseases, such as systemic lupus erythematosus (SLE), detectable erythrocyte CR1 levels are reduced, an abnormality that in part is acquired during disease activity. The loss of erythrocyte CR1 may be an important pathogenic factor in the development and severity of SLE.