The phosphatase domains of CD45 are required for ligand induced T-cell receptor downregulation
Research output: Contribution to journal › Journal article › Research › peer-review
Down-regulation of the T-cell receptor (TCR) plays an important role in modulating T-cell responses, both during T-cell development and in mature T cells. At least two distinct pathways exist for TCR down-regulation: down-regulation following TCR ligation; and down-regulation following activation of protein kinase C (PKC). Ligand-induced TCR down-regulation is dependent on protein tyrosine kinase (PTK) activity and seems to be closely related to T-cell activation. In addition, previous studies have indicated that ligand-induced TCR down-regulation is dependent on the expression of CD45, a transmembrane protein tyrosine phosphatase. The role of the different domains of CD45 in TCR down-regulation was investigated in this study. We found that the phosphatase domains of CD45 are required for efficient ligand-induced TCR down-regulation. In contrast, the extracellular domain of CD45 is dispensable for ligand-mediated TCR down-regulation. Finally, PKC-mediated TCR down-regulation was found to be independent of both the extra-and intracellular domains of CD45.
Original language | English |
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Journal | Scandinavian Journal of Immunology |
Volume | 51 |
Issue number | 5 |
Pages (from-to) | 491-6 |
Number of pages | 5 |
ISSN | 0300-9475 |
Publication status | Published - 2000 |
Bibliographical note
Keywords: Antigens, CD45; Binding Sites; Extracellular Space; Humans; Intracellular Fluid; Jurkat Cells; Ligands; Phosphoric Monoester Hydrolases; Phosphorylation; Protein Kinase C; Receptors, Antigen, T-Cell; Tyrosine
ID: 8545075