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TCRß Chains Associate with the Plasma Membrane Independently of CD3 and TCR Chains in Murine Primary T Cells¹

Jian Zhang^2,*, Konstantin Salojin^2,*, Jian-Xin Gao^*, Mark Cameron^*, Carsten Geisler^§ and Terry L. Delovitch^3,*,,

^* Autoimmunity/Diabetes Group, The John P. Robarts Research Institute, and Departments of Microbiology and Immunology and Medicine, University of Western Ontario, London, Ontario, Canada; and ^§ Institute of Medical Microbiology and Immunology, University of Copenhagen, The Panum Institute, Blegdamsvej, Copenhagen, Denmark

The TCR is a multisubunit complex composed of the clonotypic /ß disulfide-linked heterodimer and noncovalently linked invariant CD3 and CD3 and TCR chains. Recent studies demonstrate that the surface expression of CD3 components can occur independently of the clonotypic TCR complexes in both thymocytes and splenic T cells. In this study, we report that free noncovalently associated TCRß heterodimers that exist independently of CD3 and TCR chains are expressed on the cell surface of immature thymocytes and peripheral T cells, but not of T cell lines and T cell hybridomas. This suggests that the regulation of surface expression of TCRß heterodimers differs between primary T cells and T cell lines or T cell hybridomas. The isolation and biochemical characterization of surface clonotype-independent CD3 complexes and free membrane-associated TCRß complexes may provide a structural basis for the quantitative difference in amount of T cell proliferation stimulated by anti-CD3 and anti-TCRß.

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