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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.

SUBMITTER: Kemper C 

PROVIDER: S-EPMC2628304 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Properdin: New roles in pattern recognition and target clearance.

Kemper Claudia C   Hourcade Dennis E DE  

Molecular immunology 20080808 16


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  ...[more]

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