Abstract
The phagocytosis of pathogens is a critical event in host defense, not only for clearance of the invading microorganism, but also for the subsequent immune response. We have examined Dectin-1, a proinflammatory nonopsonic receptor for β-glucans, and show that it mediates the internalization of β-glucan-bearing ligands, including yeast particles. Although requiring tyrosine phosphorylation and the cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM)-like motif, uptake mediated by Dectin-1 was different from any previously reported phagocytic receptor and was not dependent on Syk-kinase in macrophages. Furthermore, intracellular trafficking of this receptor was influenced by the nature of the β-glucan ligand, which has significance for the biologic activity of these immunomodulatory carbohydrates.
| Original language | English |
|---|---|
| Pages (from-to) | 4038-4045 |
| Number of pages | 8 |
| Journal | Blood |
| Volume | 104 |
| Issue number | 13 |
| DOIs | |
| State | Published - 15 12 2004 |
| Externally published | Yes |
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