rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
2
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pubmed:dateCreated |
1995-4-6
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pubmed:abstractText |
The CD7 40-kDa glycoprotein is present on a major subset of human T cells and in the presence of phorbol esters mediates an accessory pathway of T cell activation. Hitherto, the intracellular events elicited by CD7 have been ill-defined. This report demonstrates that cross-linking of CD7 results in the formation of phosphatidic acid in the absence of phosphatidylinositol-4,5-bisphosphate metabolism and also the formation of D-3 phosphoinositides lipids which have been postulated to act as intracellular regulatory molecules. The magnitude of D-3 phosphoinositide formation was similar to that induced by CD3. Both the CD7- and CD3-induced elevation of phosphatidylinositol 3,4,5-trisphosphate approximately 5-10 fold less than that elicited by ligation of the costimulatory molecule CD28 by its counter receptor CD80. The formation of D-3 phosphoinositides following ligation of CD7 coincided with the co-association of CD7 with phosphoinositide 3-kinase, the enzyme which mediates the formation of D-3 phosphoinositide lipids. In contrast, ligation of another reported T cell accessory molecule CD5, failed to elicit formation of D-3 phosphoinositides, implying that phosphoinositide 3-kinase is not coupled to all T cell molecules with accessory functions. Since D-3 phosphoinositides have been suggested to play a pivotal role in T cell costimulatory signals induced by CD28, the results presented in this study suggest that CD7 may also influence T cell activation via this pathway.
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pubmed:grant |
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD28,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD5,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD7,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0014-2980
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
25
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
502-7
|
pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7533088-Androstadienes,
pubmed-meshheading:7533088-Animals,
pubmed-meshheading:7533088-Antibodies, Monoclonal,
pubmed-meshheading:7533088-Antigens, CD,
pubmed-meshheading:7533088-Antigens, CD28,
pubmed-meshheading:7533088-Antigens, CD5,
pubmed-meshheading:7533088-Antigens, CD7,
pubmed-meshheading:7533088-Antigens, Differentiation, T-Lymphocyte,
pubmed-meshheading:7533088-CHO Cells,
pubmed-meshheading:7533088-Cricetinae,
pubmed-meshheading:7533088-Humans,
pubmed-meshheading:7533088-Lymphocyte Activation,
pubmed-meshheading:7533088-Phosphatidic Acids,
pubmed-meshheading:7533088-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:7533088-Phosphatidylinositol Phosphates,
pubmed-meshheading:7533088-Phosphatidylinositols,
pubmed-meshheading:7533088-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:7533088-T-Lymphocytes
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pubmed:year |
1995
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pubmed:articleTitle |
Antibody ligation of CD7 leads to association with phosphoinositide 3-kinase and phosphatidylinositol 3,4,5-trisphosphate formation in T lymphocytes.
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pubmed:affiliation |
Department of Pharmacology, University of Bath, Avon, Great Britain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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