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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1996-3-18
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pubmed:abstractText |
Protein tyrosine kinase p59fyn (Fyn) associates with the TCR-CD3 complex, which suggests that Fyn plays a significant role in the signal transduction involving TCR complex. In addition to cellular genes, viral promoters such as the HIV long terminal repeat (LTR) are also activated upon T cell activation. To elucidate the functional significance of Fyn in the expression of viral promoters, we transfected a Fyn-expression vector together with a reporter plasmid containing the chloramphenicol acetyltransferase gene driven by HIV LTR into a human T cell line, Jurkat. In this assay, Fyn stimulated the promoter in HIV LTR when the transfected cells were treated with both concanavalin A and PMA as an antigen-mimic stimulation. This activation required the intact SH2 domain of Fyn. Mutational analysis of HIV LTR showed that the NF kappa B binding sites were responsible for this effect. Electrophoretic mobility shift assays and UV cross-linking experiments showed that activation of T cells by anti-CD3 antibody induced four kappa B-binding proteins (50, 60, 65 and 100 kDa) in Fyn-overexpressing cells more efficiently than in the parental cells. Our results suggested that Fyn was able to regulate expression of a subset of genes via kappa B-binding proteins upon T cell activation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FYN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1851-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8580083-Base Sequence,
pubmed-meshheading:8580083-Binding Sites,
pubmed-meshheading:8580083-DNA-Binding Proteins,
pubmed-meshheading:8580083-Gene Expression Regulation,
pubmed-meshheading:8580083-HIV,
pubmed-meshheading:8580083-Humans,
pubmed-meshheading:8580083-Leukemia, T-Cell,
pubmed-meshheading:8580083-Molecular Sequence Data,
pubmed-meshheading:8580083-NF-kappa B,
pubmed-meshheading:8580083-Promoter Regions, Genetic,
pubmed-meshheading:8580083-Protein-Tyrosine Kinases,
pubmed-meshheading:8580083-Proto-Oncogene Proteins,
pubmed-meshheading:8580083-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:8580083-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8580083-Transcription, Genetic,
pubmed-meshheading:8580083-Transcriptional Activation,
pubmed-meshheading:8580083-Tumor Cells, Cultured
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pubmed:year |
1995
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pubmed:articleTitle |
The protein tyrosine kinase Fyn activates transcription from the HIV promoter via activation of NF kappa B-like DNA-binding proteins.
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pubmed:affiliation |
Department of Oncology, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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