Jun Zhang, Theodora W. Salcedo, Xiaochun Wan, Stephen Ullrich, Bugen Hu, Theresa Gregorio, Ping Feng, Shijie Qi, Huifang Chen, Yun Hee Cho, Yuling Li, Paul A. Moore, Jiangping Wu
J Clin Invest.
2001;
107(11):1459–1468
doi:10.1172/JCI12159
This article Copyright © 2001, The American Society for Clinical Investigation
Abstract
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T
R6 (DcR3) is a new member of the TNF receptor (TNFR) family that lacks a transmembrane domain in its sequence, indicating that it is a secreted molecule. TR6 can bind to FasL and prevent FasL-induced apoptosis; it can also associate with LIGHT, another TNF family member. The role of TR6 in immune responses was investigated in this study. According to flow cytometry, recombinant human TR6-Fc binds to human LIGHT expressed on 293 cells or on activated human T cells and competes with the LIGHT receptor TR2 for the binding to LIGHT on these cells. Human TR6 could cross-react with mouse LIGHT in immunoprecipitation. TR6-Fc also downregulates cytotoxic T lymphocyte activity in vitro and graft-versus-host responses in mice. Moreover, TR6-Fc modulates lymphokine production by alloantigen-stimulated mouse T cells. TR6-Fc ameliorated rejection response to mouse heart allograft. These results indicate that TR6 can dampen T-cell responses to alloantigens. Such regulatory effects of TR6 probably occur via interference with interaction between pairs of related TNF and TNFR family members, LIGHT/TR2 being one of the possible candidate pairs.
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