Decay acceleration of the complement alternative pathway C3 convertase

Immunopharmacology. 1999 May;42(1-3):167-73. doi: 10.1016/s0162-3109(99)00005-3.


An ELISA-based method is described for analyzing the mechanism by which the decay of the alternative pathway C3 convertase is accelerated by C3 regulatory proteins. Using this assay, we show that human decay-accelerating factor (DAF) and factor H are active on mature convertase complexes (C3bBb) but not on their nascent precursor (C3bB). This finding has implications on the mechanisms of action of these two regulators. The complement convertases cleave the serum protein C3, and the resulting C3b activation fragments covalently attach to nearby targets where they direct antigen selection, immune clearance, and cell lysis. Several proteins, including the membrane protein DAF, and the serum protein factor H, limit convertase activity by promoting their irreversible dissociation. An understanding of the biochemical mechanisms providing for their activities would be helpful for the therapeutic control of the complement response.

MeSH terms

  • CD55 Antigens / immunology
  • CD55 Antigens / metabolism*
  • Complement C3-C5 Convertases / immunology
  • Complement C3-C5 Convertases / metabolism*
  • Complement Factor H / genetics
  • Complement Factor H / immunology
  • Complement Factor H / metabolism
  • Complement Pathway, Alternative / immunology
  • Complement Pathway, Alternative / physiology*
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Immune Adherence Reaction
  • Kinetics
  • Mutagenesis, Site-Directed


  • CD55 Antigens
  • CFH protein, human
  • Complement Factor H
  • Complement C3-C5 Convertases