Aarhus University Seal / Aarhus Universitets segl

Jens Christian Jensenius

Release of immune complexes bound to erythrocyte complement receptor (CR1), with particular reference to the role of factor I

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

The release of 125I-bovine serum albumin (BSA)-anti-BSA immune complexes (IC) bound to human erythrocyte complement receptors (E-CR1) was studied. IC were complement-solubilized in normal human serum (NHS), and reacted with human erythrocytes at conditions optimal for binding of the IC to E-CR1. E-CR1-bound IC could be released by the addition of NHS or purified factor I. Factor I-deficient or I-depleted serum mediated no release, and addition of purified factor I restored the release. Factor H was not required for the release of IC. The kinetics of IC release was influenced by the NHS concentration, the presence of EDTA, and the time of prior storage of the erythrocytes at 4 degrees C. NHS (1:5 to 1:10) in the presence of EDTA caused nearly maximal release within 10-20 min at 37 degrees C. In the absence of EDTA the NHS-induced IC release was markedly slower. IC released within the first 30 min showed significant rebinding to new E. The release of IC was not associated with loss of the IC binding activity of E-CR1. The NHS-mediated release of IC could be inhibited by rabbit anti-CR1 and by a mixture of protease inhibitors. Release induced by purified factor I was also inhibited by protease inhibitors. The affinity of IC binding to E-CR1 was reduced after cleavage of CR1-bound C3b-IC to iC3b-IC by factor I.
Original languageEnglish
JournalScandinavian Journal of Immunology
Pages (from-to)205-13
Number of pages9
Publication statusPublished - 1986

    Research areas

  • Antigen-Antibody Complex, Antigen-Antibody Reactions, Complement C3b, Complement Factor I, Edetic Acid, Endopeptidases, Erythrocyte Membrane, Humans, Kinetics, Protease Inhibitors, Receptors, Complement

See relations at Aarhus University Citationformats

ID: 43923909