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• W2085677677 endingPage "1937" @default.
• W2085677677 startingPage "1926" @default.
• W2085677677 abstract "The interactions between peptide/MHC complexes and their cognate TCR are essential for various T cell responses. However, the relationship between the avidity of TCR ligand and the subsequent intracellular signaling through the TCR is still unclear. To investigate the effects of TCR ligand avidity on TCR-mediated signaling, we established L cells expressing HLA-DR4 molecules covalently linked with agonistic peptide (high-affinity ligand) or altered peptide ligand (APL; low-affinity ligand) at various densities as APC for a cognate human CD4+ T cell clone. Using this system, we demonstrated that the T cell clone stimulated with APL/HLA-DR4 complexes presented at an excessive density provoked the up-regulation of CD69, IL-2 production and proliferation, but no detectable phosphorylation of ZAP-70/LAT/SLP-76. Furthermore, in contrast to the high-affinity stimulation, the low-affinity stimulation evoked delayed and sustained activation of the B-Raf/extracellular signal-regulated kinase (ERK) pathway without Raf-1 activation. The strength and duration of B-Raf/ERK activations closely correlated with the density of the TCR ligand. A knockdown approach confirmed that B-Raf activation was indispensable for the APL-induced T cell responses. These observations suggest that the differences in TCR-peptide/MHC interactions reflect the strength and duration of B-Raf/Raf-1/ERK activation in the human CD4+ T cells." @default.
• W2085677677 created "2016-06-24" @default.
• W2085677677 creator A5046865992 @default.
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• W2085677677 date "2006-07-01" @default.
• W2085677677 modified "2023-09-24" @default.
• W2085677677 title "TCR ligand avidity determines the modeof B-Raf/Raf-1/ERK activation leading to the activationof human CD4+ T cell clone" @default.
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• W2085677677 doi "https://doi.org/10.1002/eji.200535803" @default.
• W2085677677 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16791876" @default.
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