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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-2-24
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pubmed:abstractText |
We previously reported the fusion of the TEL gene to the Syk gene in myelodysplastic syndrome with t(9;12)(q22;p12). TEL-Syk fusion transformed interleukin-3 (IL-3)-dependent murine hematopoietic cell line BaF3 to growth factor independence. Here, we investigate the intracellular signal transduction of the stable transfectants. TEL-Syk fusion protein was associated with the p85 subunit of phosphatidyl inositol 3 kinase (PI3-K) followed by the activation of Akt in the absence of IL-3. Vav, phospholipase C-gamma2 and mitogen-activated protein kinase (MAPK) were also constitutively activated. TEL-Syk also activated the signal transducer and activator of transcription 5 (STAT5) in the absence of Janus kinase 2 activation. None of these kinases were phosphorylated in the BaF3 cells transfected with TELDeltaPNT-Syk in which the oligomerization domain of TEL was deleted. Inhibitor analysis showed that the MAPK pathway was important in TEL-Syk-mediated cell proliferation. The immunofluorescence technique revealed that the TEL-Syk fusion protein was located in the cytoplasm. These data suggest that TEL-Syk fusion protein in the cytoplasm leads to the constitutive activation of PI3-K/Akt, MAPK and STAT5 signal pathways, which are closely involved in IL-3-independent cell proliferation of BaF3 cells.
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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/AKT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ETS translocation variant 6 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/JAK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Milk Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
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-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-ets,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STAT5 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0887-6924
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
548-55
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:14749700-Amino Acid Substitution,
pubmed-meshheading:14749700-Cell Division,
pubmed-meshheading:14749700-Cell Line,
pubmed-meshheading:14749700-Cell Survival,
pubmed-meshheading:14749700-DNA-Binding Proteins,
pubmed-meshheading:14749700-Enzyme Precursors,
pubmed-meshheading:14749700-Humans,
pubmed-meshheading:14749700-Interleukin-3,
pubmed-meshheading:14749700-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:14749700-Janus Kinase 2,
pubmed-meshheading:14749700-Kinetics,
pubmed-meshheading:14749700-Milk Proteins,
pubmed-meshheading:14749700-Mitogen-Activated Protein Kinases,
pubmed-meshheading:14749700-Mutagenesis, Site-Directed,
pubmed-meshheading:14749700-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:14749700-Phosphorylation,
pubmed-meshheading:14749700-Protein-Serine-Threonine Kinases,
pubmed-meshheading:14749700-Protein-Tyrosine Kinases,
pubmed-meshheading:14749700-Proto-Oncogene Proteins,
pubmed-meshheading:14749700-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:14749700-Proto-Oncogene Proteins c-ets,
pubmed-meshheading:14749700-Recombinant Fusion Proteins,
pubmed-meshheading:14749700-Repressor Proteins,
pubmed-meshheading:14749700-STAT5 Transcription Factor,
pubmed-meshheading:14749700-Signal Transduction,
pubmed-meshheading:14749700-Trans-Activators,
pubmed-meshheading:14749700-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
TEL-Syk fusion constitutively activates PI3-K/Akt, MAPK and JAK2-independent STAT5 signal pathways.
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pubmed:affiliation |
Department of Hematology, Graduate School of Medicine, Nagoya University, Nagoya, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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