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  • Title: Rapid endocytosis of soluble immune complexes by Fc receptors of normal human neutrophils.
    Author: An T.
    Journal: Immunology; 1982 Mar; 45(3):413-22. PubMed ID: 7061104.
    Abstract:
    The redistribution of the Fc receptor (FcR) on human neutrophils was examined by using specific ligands made of one ferritin (Fer) molecule and one IgG antibody. Incubating neutrophils with the bound ligands at 37°, the numbers of neutrophils carrying the ligands were rapidly decreased, which was detected with a modified Coombs' mixed antiglobulin reaction (double-coating indirect rosette formation). Only less than half of the remaining rosetting neutrophils formed capping, adhering indicator red cells over one half or less of the neutrophil surface. The general trends were basically similar, even by using a second antibody to cross-link the bound ligands or incubating the coated neutrophils at 22°. By electron microscopy under the same conditions without the cross-linking antibody, the ligands were seen to be rapidly endocytosed into pinosomes at 5 min at 37° which subsequently fused with lysosomes at 15 min. No aggregation or polar capping of FcR patches was recognized. While the ligands were closely adherent to the cell membrane at 0°, some of them were released into the lumens of endocytic vesicles at 37°, suggesting the dissociation from the membrane receptors. In incubated coated cells at 22°, the general patterns of the ligand redistribution were similar except for the slower progression than at 37°. With cross-linking antibody, the patterns of endocytosis at both temperatures were similar except for the appearance of remaining FcR patches on the external cell surface. The receptor-mediated endocytosis of the ligands differed and did not result from fluid phase pinocytosis of plain Fer. Our findings are discussed with relation to the ligand-induced redistribution of other surface receptors involved in specific cellular functions.
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