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Regulation of NK cells through the 80‐kDa TNFR (CD120b)
Author(s) -
Mason Anna T.,
McVicar Daniel W.,
Smith Craig A.,
Young Howard A.,
Ware Carl F.,
Ortaldo John R.
Publication year - 1995
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.58.2.249
Subject(s) - biology , lymphokine activated killer cell , lymphokine , cytotoxic t cell , interleukin 21 , il 2 receptor , interleukin 12 , microbiology and biotechnology , tumor necrosis factor alpha , interleukin 2 , k562 cells , cytokine , immunology , antigen , in vitro , biochemistry , leukemia
By using monoclonal antibody specific for tumor necrosis factor receptor 80 (TNFR 80 ) (CD120b) and TNFRβo (CD 120a), we determined which receptor transduces the signals involved in activating natural killer (NK) cells. Purified CD56 + CD3 ‐ large lymphocytes express TNFR 80 but not TNFR 60 and interleukin‐2 (IL‐2) up‐regulates TNFR 80 expression, consistent with NK cells being activated in vivo. Treatment of NK cells with anti‐TNFR 80 for 18 h enhanced the NK activity detected on K562 target cells mimicking the effect of TNF. In combination with IL‐2, TNF enhanced the development of lymphokine‐activated killing. However, only anti‐TNFR 80 abrogated IL‐2 induction of lymphokine‐activated killer cell activity. The activity of TNF or anti‐TNFR 80 was selective for NK cytotoxic function because they did not directly mimic IL‐2 activation or induce significant proliferation, expression of cell surface activation antigens (CD25 or HLA‐DR), or interferon‐γ secretion. These results indicate that TNFR 80 is an important signal transducing receptor for the differentiation of NK cells induced by TNF and IL‐2. J. Leukoc. Biol. 58: 249–255; 1995.