Properdin: New roles in pattern recognition and target clearance

Claudia Kemper, Dennis E. Hourcade

Research output: Contribution to journalReview articlepeer-review

80 Scopus citations


Properdinwas first described over 50 years ago by Louis Pillemer and his collaborators as a vitalcomponent of an antibody-independent complement activation pathway. In the 1970s properdin was shown to be a stabilizing component of the alternative pathway convertases, the central enzymes of the complement cascade. Recently we have reported that properdin can also bind to target cells and microbes, provide a platform for convertase assembly and function, and promote target phagocytosis. Evidence is emerging that suggests that properdin interacts with a network of target ligands, phagocyte receptors, and serum regulators. Here we review the new findings and their possible implications.

Original languageEnglish
Pages (from-to)4048-4056
Number of pages9
JournalMolecular Immunology
Issue number16
StatePublished - Oct 2008


  • Apoptosis
  • Complement
  • Complement alternative pathway
  • Glycosaminoglycans
  • Neutrophils
  • Pattern recognition
  • Phagocytosis
  • Properdin


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