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rdf:type |
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lifeskim:mentions |
umls-concept:C0021756,
umls-concept:C0079773,
umls-concept:C0205263,
umls-concept:C0851285,
umls-concept:C0883208,
umls-concept:C1155551,
umls-concept:C1335280,
umls-concept:C1335875,
umls-concept:C1367307,
umls-concept:C1519726,
umls-concept:C1705050
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pubmed:issue |
4
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pubmed:dateCreated |
2003-1-24
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pubmed:abstractText |
The phosphotyrosine phosphatase SHP2 has been suggested to regulate activation of MAPK, Stat3, and Stat5 in several experimental models. In this study we investigated the role of SHP2 in IL-2 induced activation of MAPK and the Stat proteins using the human CTCL cell line MyLa2059 derived from a cutaneous T cell lymphoma (CTCL). For this purpose, MyLa2059 cells were stably transfected with wild-type SHP2 or inactive SHP2. The cells transfected with inactive SHP2 showed reduced MAPK activation upon IL-2 stimulation, suggesting that SHP2 upregulates IL-2 induced MAPK activation in T cells. However, the constitutive tyrosine phosphorylation of Stat3 as well as IL-2 induced Stat5 tyrosine phosphorylation and DNA binding were unaffected by the stably transfected wild-type SHP2 as well as the inactive SHP2. In conclusion, we show for the first time that SHP2 positively regulates IL-2 induced MAPK activation in malignant T cells. Furthermore, the results indicate that SHP2 may not be involved in the activation of Stat3 or Stat5 in CTCL cells.
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pubmed:grant |
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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/DNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/MAP3K1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Milk Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 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/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion 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/STAT5 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1043-4666
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-7
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:12543077-Amino Acid Substitution,
pubmed-meshheading:12543077-DNA, Neoplasm,
pubmed-meshheading:12543077-DNA-Binding Proteins,
pubmed-meshheading:12543077-Enzyme Activation,
pubmed-meshheading:12543077-Humans,
pubmed-meshheading:12543077-Interleukin-2,
pubmed-meshheading:12543077-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:12543077-MAP Kinase Kinase Kinase 1,
pubmed-meshheading:12543077-MAP Kinase Signaling System,
pubmed-meshheading:12543077-Milk Proteins,
pubmed-meshheading:12543077-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:12543077-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:12543077-Mitogen-Activated Protein Kinases,
pubmed-meshheading:12543077-Mutation, Missense,
pubmed-meshheading:12543077-Mycosis Fungoides,
pubmed-meshheading:12543077-Neoplasm Proteins,
pubmed-meshheading:12543077-Phosphorylation,
pubmed-meshheading:12543077-Protein Binding,
pubmed-meshheading:12543077-Protein Processing, Post-Translational,
pubmed-meshheading:12543077-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:12543077-Protein Tyrosine Phosphatases,
pubmed-meshheading:12543077-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12543077-Recombinant Fusion Proteins,
pubmed-meshheading:12543077-STAT3 Transcription Factor,
pubmed-meshheading:12543077-STAT5 Transcription Factor,
pubmed-meshheading:12543077-Trans-Activators,
pubmed-meshheading:12543077-Transfection,
pubmed-meshheading:12543077-Tumor Cells, Cultured
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pubmed:year |
2002
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pubmed:articleTitle |
SHP2 regulates IL-2 induced MAPK activation, but not Stat3 or Stat5 tyrosine phosphorylation, in cutaneous T cell lymphoma cells.
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pubmed:affiliation |
Institute of Medical Microbiology and Immunology, University of Copenhagen, Blegdamsvej 3c, 2200 Copenhagen-N, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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