Abstract
T LYMPHOCYTES can be activated by various stimuli directed either against the T-cell antigen receptor–CD3 antigen complex (Ti–CD3) or the CD2 molecule; see ref.1 for a review. Activation signals generated by antigen binding to the antigen-specific α/β heterodimer (Ti) are thought to be transduced via the invariant CD3 γ, ε and δchains, and the associatedζ and η subunits2,3. The physiological role of the interaction of CD2 with its homologous cell-surface associated ligand LFA-34,5remains to be fully elucidated. It has been suggested that CD2 regulates an antigen-independent pathway of activation6or that signals delivered via CD2 are an integral part of the antigen-specific pathway7–10. Several recent studies have indicated a requirement for the Ti–CD3 complex in CD2 signalling. Thus, mutant T-cell lines expressing CD2, but not Ti–CD3, on the cell surface cannot be activated via the CD2 molecules9,10. Functional interaction between the Ti–CD3 complex and the CD2 antigen suggests that these T-lymphocyte cell-surface structures are physically associated. Here we use a digitonin-based solubilization procedure to explore this possibility and show that 40% of the cell-surface CD2 molecules can be specifically co-precipitated in association with the Ti–CD3 complex.
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Brown, M., Cantrell, D., Brattsand, G. et al. The CD2 antigen associates with the T-cell antigen receptor CD3 antigen complex on the surface of human T lymphocytes. Nature 339, 551–553 (1989). https://doi.org/10.1038/339551a0
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DOI: https://doi.org/10.1038/339551a0
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