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Association with FcRgamma is essential for activation signal through NKR-P1 (CD161) in natural killer (NK) cells and NK1.1+ T cells.

Arase N, Arase H, Park SY, Ohno H, Ra C, Saito T - J. Exp. Med. (1997)

Bottom Line: In this study, we analyzed the cell surface complex associated with NKR-P1 on NK cells and found that NKR-P1 associates with the FcRgamma chain which is an essential component of Fc receptors for IgG and IgE.Similarly, NK1.1+ T cells from FcRgamma-deficient mice did not produce IFN-gamma upon NKR-P1 crosslinking.These findings demonstrate that the FcRgamma chain plays an important role in activation of NK cells via the NKR-P1 molecule.

View Article: PubMed Central - PubMed

Affiliation: Division of Molecular Genetics, Center for Biological Science, Chiba University School of Medicine, Chiba 260, Japan.

ABSTRACT
Natural killer (NK) cells exhibit cytotoxicity against variety of tumor cells and virus-infected cells without prior sensitization and represent unique lymphocytes involved in primary host defense. NKR-P1 is thought to be one of NK receptors mediating activation signals because cross-linking of NKR-P1 activates NK cells to exhibit cytotoxicity and IFN-gamma production. However, molecular mechanism of NK cell activation via NKR-P1 is not well elucidated. In this study, we analyzed the cell surface complex associated with NKR-P1 on NK cells and found that NKR-P1 associates with the FcRgamma chain which is an essential component of Fc receptors for IgG and IgE. The association between FcRgamma and NKR-P1 is independent of Fc receptor complexes. Furthermore, NK cells from FcRgamma-deficient mice did not show cytotoxicity or IFN-gamma production upon NKR-P1 cross-linking. Similarly, NK1.1+ T cells from FcRgamma-deficient mice did not produce IFN-gamma upon NKR-P1 crosslinking. These findings demonstrate that the FcRgamma chain plays an important role in activation of NK cells via the NKR-P1 molecule.

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Loss of the cell surface expression of FcγRIII on NK cells  from γ−/− mice. CD4−CD8−HSA−sIg− splenocytes from γ+/+, γ+/− and  γ−/− mice were cultured for 4 d in the presence of 1,000 U/ml IL-2. The  cultured cells were stained with FITC–anti-FcγRIII, PE–anti-NK1.1 and  Quantum red-anti-CD3ε mAbs and the expression of FcγRIII and  NK1.1 on the CD3− population was illustrated. Representative data from  five independent experiments are shown.
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Figure 3: Loss of the cell surface expression of FcγRIII on NK cells from γ−/− mice. CD4−CD8−HSA−sIg− splenocytes from γ+/+, γ+/− and γ−/− mice were cultured for 4 d in the presence of 1,000 U/ml IL-2. The cultured cells were stained with FITC–anti-FcγRIII, PE–anti-NK1.1 and Quantum red-anti-CD3ε mAbs and the expression of FcγRIII and NK1.1 on the CD3− population was illustrated. Representative data from five independent experiments are shown.

Mentions: To elucidate the physiological role of the association between FcRγ and NKR-P1 particularly on signal transduction in NK cells, NK cells were prepared from γ−/− mice and analyzed for NKR-P1 expression and NKR-P1–mediated NK cell activation. When CD4−CD8−sIg− splenocytes from γ−/− mice were stained with anti-NK1.1 and anti-CD3ε mAbs, normal development of NK cells (NK1.1+CD3−) was observed (data not shown). When expression of FcγRIII on IL-2–expanded NK cells was analyzed, NK cells from γ−/− mice did not express FcγRIII (Fig. 3). In addition, the expression level of NK1.1 on the cell surface of IL-2–expanded NK cells from γ−/− mice was significantly lower than that of NK cells from γ+/+ and γ+/− mice. However, the difference of NK1.1 expression between γ−/− and γ+/− mice was marginal when freshly isolated NK cells were analyzed (data not shown). This suggested that FcRγ is not absolutely required for but affects the surface expression of the NKR-P1 molecule.


Association with FcRgamma is essential for activation signal through NKR-P1 (CD161) in natural killer (NK) cells and NK1.1+ T cells.

Arase N, Arase H, Park SY, Ohno H, Ra C, Saito T - J. Exp. Med. (1997)

Loss of the cell surface expression of FcγRIII on NK cells  from γ−/− mice. CD4−CD8−HSA−sIg− splenocytes from γ+/+, γ+/− and  γ−/− mice were cultured for 4 d in the presence of 1,000 U/ml IL-2. The  cultured cells were stained with FITC–anti-FcγRIII, PE–anti-NK1.1 and  Quantum red-anti-CD3ε mAbs and the expression of FcγRIII and  NK1.1 on the CD3− population was illustrated. Representative data from  five independent experiments are shown.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2199168&req=5

Figure 3: Loss of the cell surface expression of FcγRIII on NK cells from γ−/− mice. CD4−CD8−HSA−sIg− splenocytes from γ+/+, γ+/− and γ−/− mice were cultured for 4 d in the presence of 1,000 U/ml IL-2. The cultured cells were stained with FITC–anti-FcγRIII, PE–anti-NK1.1 and Quantum red-anti-CD3ε mAbs and the expression of FcγRIII and NK1.1 on the CD3− population was illustrated. Representative data from five independent experiments are shown.
Mentions: To elucidate the physiological role of the association between FcRγ and NKR-P1 particularly on signal transduction in NK cells, NK cells were prepared from γ−/− mice and analyzed for NKR-P1 expression and NKR-P1–mediated NK cell activation. When CD4−CD8−sIg− splenocytes from γ−/− mice were stained with anti-NK1.1 and anti-CD3ε mAbs, normal development of NK cells (NK1.1+CD3−) was observed (data not shown). When expression of FcγRIII on IL-2–expanded NK cells was analyzed, NK cells from γ−/− mice did not express FcγRIII (Fig. 3). In addition, the expression level of NK1.1 on the cell surface of IL-2–expanded NK cells from γ−/− mice was significantly lower than that of NK cells from γ+/+ and γ+/− mice. However, the difference of NK1.1 expression between γ−/− and γ+/− mice was marginal when freshly isolated NK cells were analyzed (data not shown). This suggested that FcRγ is not absolutely required for but affects the surface expression of the NKR-P1 molecule.

Bottom Line: In this study, we analyzed the cell surface complex associated with NKR-P1 on NK cells and found that NKR-P1 associates with the FcRgamma chain which is an essential component of Fc receptors for IgG and IgE.Similarly, NK1.1+ T cells from FcRgamma-deficient mice did not produce IFN-gamma upon NKR-P1 crosslinking.These findings demonstrate that the FcRgamma chain plays an important role in activation of NK cells via the NKR-P1 molecule.

View Article: PubMed Central - PubMed

Affiliation: Division of Molecular Genetics, Center for Biological Science, Chiba University School of Medicine, Chiba 260, Japan.

ABSTRACT
Natural killer (NK) cells exhibit cytotoxicity against variety of tumor cells and virus-infected cells without prior sensitization and represent unique lymphocytes involved in primary host defense. NKR-P1 is thought to be one of NK receptors mediating activation signals because cross-linking of NKR-P1 activates NK cells to exhibit cytotoxicity and IFN-gamma production. However, molecular mechanism of NK cell activation via NKR-P1 is not well elucidated. In this study, we analyzed the cell surface complex associated with NKR-P1 on NK cells and found that NKR-P1 associates with the FcRgamma chain which is an essential component of Fc receptors for IgG and IgE. The association between FcRgamma and NKR-P1 is independent of Fc receptor complexes. Furthermore, NK cells from FcRgamma-deficient mice did not show cytotoxicity or IFN-gamma production upon NKR-P1 cross-linking. Similarly, NK1.1+ T cells from FcRgamma-deficient mice did not produce IFN-gamma upon NKR-P1 crosslinking. These findings demonstrate that the FcRgamma chain plays an important role in activation of NK cells via the NKR-P1 molecule.

Show MeSH
Related in: MedlinePlus