The phosphatidylinositol phosphatase PTEN is under control of costimulation and regulates proliferation in human T cells

Eur J Immunol. 2002 Apr;32(4):1196-204. doi: 10.1002/1521-4141(200204)32:4<1196::AID-IMMU1196>3.0.CO;2-K.

Abstract

The phosphatidylinositol phosphatase gene PTEN is a dual specific phosphatase acting on phospho amino acids but also on three phosphorylated inositol phospholipids. Present results demonstrate that PTEN is inducible by costimulatory signals in human CD4(+) T cells. PTEN expression was up-regulated on RNA and protein level in freshly isolated human CD4(+) T cells following stimulation with CD28 or CD2. In contrast, PTEN expression was high but remained CD28 and CD2 unresponsive in lymphoma cells. Intracellular staining revealed PTEN expression in CD4(+) T cell populations stimulated with anti-CD28 or anti-CD28 / anti-CD3. Stimulation with anti-CD3 alone did not induce PTEN expression. Inhibition of PTEN expression by antisense oligonucleotides in CD4(+) T cells stimulated with non-mitogenic anti-CD28 resulted in massively increased proliferation, which was sensitive to the phosphatidylinositol 3-kinase (PI3 K) inhibitor wortmannin. Although CD28 and CD2 induce PI3 K signal transduction, wortmannin did not block PTEN up-regulation by CD28 or CD2 indicating that PTEN gene expression is PI3 K independent. These results demonstrate that PTEN negatively controls costimulatory signals by antagonizing PI3 K activity in the absence of TCR engagement.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Androstadienes / pharmacology
  • CD2 Antigens / physiology*
  • CD28 Antigens / physiology*
  • CD4-Positive T-Lymphocytes / cytology
  • CD4-Positive T-Lymphocytes / enzymology*
  • Cell Cycle
  • Cell Division / physiology
  • Cells, Cultured / cytology
  • Cells, Cultured / enzymology
  • Enzyme Activation
  • Enzyme Induction
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Lymphocyte Activation
  • Lymphoma, T-Cell / genetics
  • Lymphoma, T-Cell / metabolism
  • Lymphoma, T-Cell / pathology
  • Oligodeoxyribonucleotides, Antisense / pharmacology
  • PTEN Phosphohydrolase
  • Phosphatidylinositol 3-Kinases / physiology
  • Phosphoinositide-3 Kinase Inhibitors
  • Phosphoric Monoester Hydrolases / biosynthesis
  • Phosphoric Monoester Hydrolases / genetics
  • Phosphoric Monoester Hydrolases / physiology*
  • RNA, Messenger / biosynthesis
  • Receptors, Antigen, T-Cell / immunology
  • Signal Transduction / drug effects
  • Thionucleotides / pharmacology
  • Tumor Cells, Cultured / cytology
  • Tumor Cells, Cultured / enzymology
  • Tumor Suppressor Proteins / biosynthesis
  • Tumor Suppressor Proteins / genetics
  • Tumor Suppressor Proteins / physiology*
  • Wortmannin

Substances

  • Androstadienes
  • CD2 Antigens
  • CD28 Antigens
  • Enzyme Inhibitors
  • Oligodeoxyribonucleotides, Antisense
  • Phosphoinositide-3 Kinase Inhibitors
  • RNA, Messenger
  • Receptors, Antigen, T-Cell
  • Thionucleotides
  • Tumor Suppressor Proteins
  • Phosphoric Monoester Hydrolases
  • PTEN Phosphohydrolase
  • PTEN protein, human
  • Wortmannin