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lüll Properdin: New roles in pattern recognition and target clearance Kemper C; Hourcade DEMol Immunol 2008[Oct]; 45 (16): 4048-56Properdin 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.|Animals[MESH]|Complement Pathway, Alternative/*immunology[MESH]|Complement System Proteins/*immunology/metabolism[MESH]|Humans[MESH]|Models, Immunological[MESH]|Properdin/*immunology/metabolism[MESH] |