CD95 (Fas)-dependent elimination of self-reactive B cells upon interaction with CD4+ T cells
Article Abstract:
Transgene-encoded autoantigen hen egg lysozyme (HEL)-specific CD4+ T cells induce proliferation and antibodies production by B cells which are unexposed to HEL. On the other hand, B cells which have been exposed to HEL during development are destroyed in the presence of these T cells. However, anergic B cells which do not contain CD95 are not destroyed by the T cells and proliferate instead. This removal of the self-reactive B cells from mice which are transgenic for immunoglobulin and T-cell receptor genes is probably by apoptosis of the B cells by the action of CD95 on the B cells.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Ligand-specific oligomerization of T-cell receptor molecules
Article Abstract:
It is possible to use quasi-elastic light scattering to demonstrate that TCR/peptide major histocompatability complex (MHC) molecules oligomerize in solution to form supramolecular structures where MHC molecules bound to a full agonist peptide are present. This reaction takes place at concentrations near the dissociation constant of the binding reaction. It provides clear proof for models of T-cell signalling based on the specific assembly of multiple TC/peptide-MHC complexes where the extent of assembly has an influence on the scope and qualitative nature of the transduced signal.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Serial engagement proposed
Article Abstract:
Valitutti and his colleagues have proposed a serial engagement model to explain the peculiar interaction between molecules of the major histocompatibility complex (MHC) and the T-cell receptor (TCR). TCR cell is highly sensitive but it forms few cognate ligands with the molecule of MHC. This model seeks to explain this combination of high sensitivity and low affinity. The model shows that TCR complexes disappear from the surface in numbers that are large multiples of cognate peptide.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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