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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2002-10-30
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pubmed:abstractText |
T cell activation is triggered by several hours of contact with peptide-major histocompatibility (MHC) complexes on the surface of antigen-presenting cells (APCs). The nature and location of the sustained signal transduction pathways required for T cell activation are unknown. We show here that the production of phosphatidylinositol(3,4,5)triphosphate (PIP3) was dynamically sustained for hours as T cells responded to antigen. In addition, sustained elevation of PIP3 was essential for T cell proliferation. There was PIP3 accumulation in the T cell-APC contact zone and at the antipodal pole of the cell. The immune synapse is thus not the sole site of sustained signal transduction in activated T cells.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-(4-morpholinyl)-8-phenyl-4H-1-benz...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Chromones,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/H-2 Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Morpholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Vanadates,
http://linkedlifedata.com/resource/pubmed/chemical/histocompatibility antigen H-2D(b),
http://linkedlifedata.com/resource/pubmed/chemical/pervanadate,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1529-2908
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1082-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12389042-Animals,
pubmed-meshheading:12389042-Antigen Presentation,
pubmed-meshheading:12389042-Antigens, Viral,
pubmed-meshheading:12389042-Cell Division,
pubmed-meshheading:12389042-Cell Polarity,
pubmed-meshheading:12389042-Chromones,
pubmed-meshheading:12389042-Enzyme Activation,
pubmed-meshheading:12389042-Enzyme Inhibitors,
pubmed-meshheading:12389042-Genes, Reporter,
pubmed-meshheading:12389042-Green Fluorescent Proteins,
pubmed-meshheading:12389042-H-2 Antigens,
pubmed-meshheading:12389042-Humans,
pubmed-meshheading:12389042-Luminescent Proteins,
pubmed-meshheading:12389042-Lymphocyte Activation,
pubmed-meshheading:12389042-Membrane Lipids,
pubmed-meshheading:12389042-Mice,
pubmed-meshheading:12389042-Mice, Inbred C57BL,
pubmed-meshheading:12389042-Mice, Transgenic,
pubmed-meshheading:12389042-Microscopy, Confocal,
pubmed-meshheading:12389042-Morpholines,
pubmed-meshheading:12389042-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:12389042-Phosphatidylinositol Phosphates,
pubmed-meshheading:12389042-Promoter Regions, Genetic,
pubmed-meshheading:12389042-Protein Structure, Tertiary,
pubmed-meshheading:12389042-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12389042-Proto-Oncogene Proteins,
pubmed-meshheading:12389042-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:12389042-Signal Transduction,
pubmed-meshheading:12389042-T-Lymphocyte Subsets,
pubmed-meshheading:12389042-Vanadates
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pubmed:year |
2002
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pubmed:articleTitle |
Sustained and dynamic inositol lipid metabolism inside and outside the immunological synapse.
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pubmed:affiliation |
Lymphocyte Activation Laboratory, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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