title: Properdin: New roles in pattern recognition and target clearance.
abstract: 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.
authors.affiliation: MRC Centre for Transplantation, King's College London, UK.
authors.forename: Claudia
authors.initials: C
authors.lastname: Kemper
authors.forename: Dennis E
authors.initials: DE
authors.lastname: Hourcade
mesh_terms: 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
chemical_list: D011414:Properdin; D003165:Complement System Proteins