Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-4-4
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD2, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD28, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, Antisense, http://linkedlifedata.com/resource/pubmed/chemical/PTEN Phosphohydrolase, http://linkedlifedata.com/resource/pubmed/chemical/PTEN protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell, http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1196-204
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:11932928-Adult, pubmed-meshheading:11932928-Androstadienes, pubmed-meshheading:11932928-Antigens, CD2, pubmed-meshheading:11932928-Antigens, CD28, pubmed-meshheading:11932928-CD4-Positive T-Lymphocytes, pubmed-meshheading:11932928-Cell Cycle, pubmed-meshheading:11932928-Cell Division, pubmed-meshheading:11932928-Cells, Cultured, pubmed-meshheading:11932928-Enzyme Activation, pubmed-meshheading:11932928-Enzyme Induction, pubmed-meshheading:11932928-Enzyme Inhibitors, pubmed-meshheading:11932928-Humans, pubmed-meshheading:11932928-Lymphocyte Activation, pubmed-meshheading:11932928-Lymphoma, T-Cell, pubmed-meshheading:11932928-Oligodeoxyribonucleotides, Antisense, pubmed-meshheading:11932928-PTEN Phosphohydrolase, pubmed-meshheading:11932928-Phosphatidylinositol 3-Kinases, pubmed-meshheading:11932928-Phosphoric Monoester Hydrolases, pubmed-meshheading:11932928-RNA, Messenger, pubmed-meshheading:11932928-Receptors, Antigen, T-Cell, pubmed-meshheading:11932928-Signal Transduction, pubmed-meshheading:11932928-Thionucleotides, pubmed-meshheading:11932928-Tumor Cells, Cultured, pubmed-meshheading:11932928-Tumor Suppressor Proteins
pubmed:year
2002
pubmed:articleTitle
The phosphatidylinositol phosphatase PTEN is under control of costimulation and regulates proliferation in human T cells.
pubmed:affiliation
Swiss Institute of Allergy and Asthma Research (SIAF), Davos, Switzerland. csweber@siaf.unizh.ch
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't