期刊
IMMUNITY
卷 12, 期 3, 页码 241-250出版社
CELL PRESS
DOI: 10.1016/S1074-7613(00)80177-6
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- NIAID NIH HHS [N01AI95361] Funding Source: Medline
- NIGMS NIH HHS [T32 GM08334] Funding Source: Medline
A series of novel chemically defined soluble oligomers of the human MHC class II protein HLA-DR1 was constructed to probe the molecular requirements for initiation of T cell activation. MHC dimers, trimers, and tetramers stimulated T cells, as measured by upregulation of the activation markers CD69 and CD25, and by internalization of activated T cell receptor subunits. Monomeric MHC-peptide complexes engaged T cell receptors but did not induce activation. For a given amount of receptor engagement, the extent of activation was equivalent for each of the oligomers and correlated with the number of T cell receptor cross-links induced. These results suggest that formation or rearrangement of a T cell receptor dimer is necessary and sufficient for initiation of T cell signaling.
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