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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2002-10-2
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pubmed:abstractText |
In the previous study, we demonstrated that the nuclear isoform of T-cell protein-tyrosine phosphatase (TC-PTP) dephosphorylated and deactivated signal transducer and activator of transcription 5a (STAT5a) and STAT5b, thereby negatively regulating prolactin (PRL)-mediated signaling pathway. In this study, we examined the involvement of the nuclear isoform of TC-PTP in interleukin-6 (IL-6)-mediated signaling pathway. IL-6 is a multifunctional cytokine that plays important roles in the immune system, hematopoiesis, and acute phase reactions, and has also implicated in IL-6-related diseases. Here, we demonstrate that IL-6-induced tyrosine-phosphorylation and activation of STAT3 were suppressed by overexpression of the nuclear isoform of TC-PTP in 293T cells. Tyrosine-phosphorylated STAT3 directly interacted with a substrate-trapping mutant of TC-PTP. Furthermore, retrovirus-mediated overexpression of the nuclear isoform of TC-PTP suppressed the IL-6-induced growth arrest of myeloid leukemia M1 cells. Endogenous TC-PTP complexed with STAT3 in the nucleus of M1 cells. These results strongly suggest that the nuclear isoform of TC-PTP may serve as a negative regulator of IL-6-mediated signaling pathway.
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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/Acute-Phase Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Stat3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
297
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
811-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12359225-Acute-Phase Proteins,
pubmed-meshheading:12359225-Animals,
pubmed-meshheading:12359225-Cell Division,
pubmed-meshheading:12359225-Cell Line,
pubmed-meshheading:12359225-Cell Nucleus,
pubmed-meshheading:12359225-DNA-Binding Proteins,
pubmed-meshheading:12359225-Genes, Reporter,
pubmed-meshheading:12359225-Humans,
pubmed-meshheading:12359225-Interleukin-6,
pubmed-meshheading:12359225-Isoenzymes,
pubmed-meshheading:12359225-Kinetics,
pubmed-meshheading:12359225-Luciferases,
pubmed-meshheading:12359225-Mice,
pubmed-meshheading:12359225-Phosphorylation,
pubmed-meshheading:12359225-Polymerase Chain Reaction,
pubmed-meshheading:12359225-Protein Tyrosine Phosphatase, Non-Receptor Type 2,
pubmed-meshheading:12359225-Protein Tyrosine Phosphatases,
pubmed-meshheading:12359225-Recombinant Proteins,
pubmed-meshheading:12359225-STAT3 Transcription Factor,
pubmed-meshheading:12359225-Signal Transduction,
pubmed-meshheading:12359225-Substrate Specificity,
pubmed-meshheading:12359225-Trans-Activators,
pubmed-meshheading:12359225-Transfection,
pubmed-meshheading:12359225-Tumor Cells, Cultured
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pubmed:year |
2002
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pubmed:articleTitle |
The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation.
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pubmed:affiliation |
Department of Immunology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-Ku Kita 12 Nishi 6, Sapporo 060-0812, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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