Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-4-6
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.
pubmed:grant
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
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
502-7
pubmed:dateRevised
2010-11-18
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
pubmed:year
1995
pubmed:articleTitle
Antibody ligation of CD7 leads to association with phosphoinositide 3-kinase and phosphatidylinositol 3,4,5-trisphosphate formation in T lymphocytes.
pubmed:affiliation
Department of Pharmacology, University of Bath, Avon, Great Britain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't