Abstract
The binding of multivalent immunoglobulin G complexes to Fc receptors (FcγRs) on macrophages activates multiple immune functions. A murine macrophage cell line, but not a fibroblast cell line, that was transfected with human FcγRIIA mediated phagocytosis and an intracellular Ca2+ concentration ([Ca2+]i) flux upon cross-linking of human FcγRIIA. Transfected macrophages that expressed a truncated receptor lacking 17 carboxy-terminal amino acids phagocytosed small antibody complexes. However, only wild-type transfectants phagocytosed labeled erythrocytes and fluxed [Ca2+]i. Thus, the cytoplasmic domain of human FcγRIIA contains distinct functional regions.
| Original language | English |
|---|---|
| Pages (from-to) | 1785-1788 |
| Number of pages | 4 |
| Journal | Science |
| Volume | 254 |
| Issue number | 5039 |
| DOIs | |
| State | Published - 1991 |
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