rdf:type |
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lifeskim:mentions |
umls-concept:C0037083,
umls-concept:C0086418,
umls-concept:C0530698,
umls-concept:C1314939,
umls-concept:C1334291,
umls-concept:C1335875,
umls-concept:C1704259,
umls-concept:C1705050,
umls-concept:C1705987,
umls-concept:C1710082,
umls-concept:C1879547
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pubmed:dateCreated |
1997-12-4
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pubmed:abstractText |
The JAK (Janus kinase) family of protein tyrosine kinases and the STATs (signal transducers and activators of transcription) have been shown to be activated in response to a number of cytokines and growth factors. In this study, we evaluated the activation of JAK/STAT pathway upon human interleukin-5 (hIL-5) stimulation of two different hIL-5-responsive cell lines, hIL-5 receptor alpha-subunit (hIL-5R alpha) cDNA-transfected TF-1 (TF-h5R alpha) and butyric-acid-treated YY-1 (YY-Bu), and peripheral eosinophils. Immunoprecipitation and electrophoretic mobility shift analysis revealed that tyrosine phosphorylation of JAK2 and activation of STAT5 were induced upon stimulation with hIL-5 in all three cell types, while STAT1 activation was only observed in eosinophils. These results indicate that JAK2/STAT5 activation is a common JAK/STAT pathway for hIL-5-mediated signal in these cells.
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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/Interleukin-5,
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/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-5,
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 |
Oct
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pubmed:issn |
1018-2438
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
114 Suppl 1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9363920-Cell Line,
pubmed-meshheading:9363920-DNA-Binding Proteins,
pubmed-meshheading:9363920-Eosinophils,
pubmed-meshheading:9363920-Humans,
pubmed-meshheading:9363920-Interleukin-5,
pubmed-meshheading:9363920-Janus Kinase 2,
pubmed-meshheading:9363920-Milk Proteins,
pubmed-meshheading:9363920-Protein-Tyrosine Kinases,
pubmed-meshheading:9363920-Proto-Oncogene Proteins,
pubmed-meshheading:9363920-Receptors, Interleukin,
pubmed-meshheading:9363920-Receptors, Interleukin-5,
pubmed-meshheading:9363920-STAT5 Transcription Factor,
pubmed-meshheading:9363920-Signal Transduction,
pubmed-meshheading:9363920-Trans-Activators
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pubmed:year |
1997
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pubmed:articleTitle |
The activation of the JAK2/STAT5 pathway is commonly involved in signaling through the human IL-5 receptor.
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pubmed:affiliation |
Department of Immunology, Institute of Medical Science, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article
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