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Conserved Cytoplasmic Tyrosine Residues of the γ Subunit are Required for a Phagocytic Signal Mediated by FcγRIIIA

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Author(s)
Jong-Gu ParkRichard K. MurrayPaul ChienChristine DarbyAlan D. Schreiber
Keimyung Author(s)
Park, Jong Gu
Department
Dept. of Molecular Medicine (분자의학)
Journal Title
Journal of Clinical Investigation
Issued Date
1993
Volume
92
Issue
4
Abstract
Fc receptors for immunoglobulins are found on many cells and are important in host defense. We transfected Fc gamma RIIIA, present on macrophages and natural killer (NK) cells, into COS-1 cells to study its role in phagocytosis and calcium mobilization in the absence of other Fc gamma receptors. Human Fc gamma RIIIA-alpha (CD16) was cotransfected with its associated chains, either Fc gamma RIIIA gamma or zeta. Both gamma and zeta were observed to induce a phagocytic signal, but gamma was at least sixfold more effective than zeta. Conservative substitution by phenylalanine of either one of the two cytoplasmic tyrosine residues in the gamma chain resulted in markedly diminished phagocytosis and calcium mobilization. Tyrphostin 23, an inhibitor of tyrosine kinases, reversibly inhibited phagocytosis. Further, in vitro kinase assays with the wild type and mutant gamma chains demonstrated that the wild type gamma chain, but not the mutant gamma chains, is phosphorylated. These results suggest that the cytoplasmic tyrosine residues and tyrosine phosphorylation are required for Fc gamma RIIIA to mediate two signal transduction events: phagocytosis and calcium mobilization.
Keimyung Author(s)(Kor)
박종구
Publisher
School of Medicine
Citation
Jong-Gu Park et al. (1993). Conserved Cytoplasmic Tyrosine Residues of the γ Subunit are Required for a Phagocytic Signal Mediated by FcγRIIIA. Journal of Clinical Investigation, 92(4), 2073–2079. doi: 10.1172/JCI116804
Type
Article
ISSN
0021-9738
DOI
10.1172/JCI116804
URI
https://kumel.medlib.dsmc.or.kr/handle/2015.oak/33980
Appears in Collections:
1. School of Medicine (의과대학) > Dept. of Molecular Medicine (분자의학)
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