The phosphatase domains of CD45 are required for ligand induced T-cell receptor downregulation

Scand J Immunol. 2000 May;51(5):491-6. doi: 10.1046/j.1365-3083.2000.00716.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Extracellular Space / metabolism
  • Humans
  • Intracellular Fluid / metabolism
  • Jurkat Cells
  • Leukocyte Common Antigens / metabolism*
  • Ligands
  • Phosphoric Monoester Hydrolases / metabolism*
  • Phosphorylation
  • Protein Kinase C / metabolism
  • Receptors, Antigen, T-Cell / metabolism*
  • Tyrosine / metabolism

Substances

  • Ligands
  • Receptors, Antigen, T-Cell
  • Tyrosine
  • Protein Kinase C
  • Phosphoric Monoester Hydrolases
  • Leukocyte Common Antigens