Properdin: New roles in pattern recognition and target clearance.
Properdin was first described over 50 years ago by Louis Pillemer and his collaborators as a vital component 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.
Kemper
Claudia
C
MRC Centre for Transplantation, King's College London, UK.
Hourcade
Dennis E
DE
D000818:Animals; D003170:Complement Pathway, Alternative / Q000276:immunology*; D003165:Complement System Proteins / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D018448:Models, Immunological; D011414:Properdin / Q000276:immunology* / Q000378:metabolism
D011414:Properdin; D003165:Complement System Proteins