Abstract
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 language | English |
|---|---|
| Journal | Molecular Immunology |
| Volume | 45 |
| Issue number | 16 |
| Pages (from-to) | 4048-4056 |
| Number of pages | 9 |
| ISSN | 0161-5890 |
| DOIs | |
| Publication status | Published - 10.2008 |
Funding
We gratefully acknowledge our properdin collaborators Dirk Spitzer, Lynne Mitchell, LiJuan Zhang, and John Atkinson and the helpful suggestions of Anja Fuchs, Christine Pham, Peter Densen, Michael Apicella, Tony Zalewski and Panisadee Avirutnan. We thank Madonna Bogacki for help with the manuscript. DEH was supported by NIH grant R01 AI05143. The content of this article is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of Allergy and infectious Diseases or the National Institutes of Health.
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
