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Zhang, J. et al.

Zhang, Salcedo, Wan, Ullrich, Hu, Gregorio, Feng, Qi, Chen, Cho, Li, Moore, Wu,

Modulation of T-cell responses to alloantigens by TR6/DcR3.

TR6 (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.[1]

References

Modulation of T-cell responses to alloantigens by TR6/DcR3. Zhang, J., Salcedo, T.W., Wan, X., Ullrich, S., Hu, B., Gregorio, T., Feng, P., Qi, S., Chen, H., Cho, Y.H., Li, Y., Moore, P.A., Wu, J. J. Clin. Invest. (2001) [Pubmed]

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