|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2004-4-19
|
|
pubmed:abstractText |
NPM-ALK characterizes anaplastic large cell lymphoma (ALCL), as does the high expression of CD30, a feature shared with H-RS cells of classic Hodgkin's lymphoma. In H-RS cells, ligand-independent signaling by overexpressed CD30 drives constitutive NF-kappaB activation, which is absent in ALCL cells. Here we show that NPM-ALK impedes CD30 signaling and NF-kappaB activation, dependent on both ALK kinase activity and the N-terminal NPM domain. NPM-ALK transduction into H-RS cell lines abrogates recruitment and aggregation of TRAF proteins, inducing an ALCL-like morphology and phenotype. TRAF2 associates with NPM-ALK at a consensus binding motif located in the kinase domain. Thus, NPM-ALK abrogates CD30-driven NF-kappaB activation and can also induce an ALCL phenotype, distinguishing ALCL cells from H-RS cells of T cell origin.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD30,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/p80(NPM-ALK) protein
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1535-6108
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
5
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
353-64
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:15093542-Amino Acid Motifs,
pubmed-meshheading:15093542-Antigens, CD30,
pubmed-meshheading:15093542-Cells, Cultured,
pubmed-meshheading:15093542-Consensus Sequence,
pubmed-meshheading:15093542-Cytoplasm,
pubmed-meshheading:15093542-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:15093542-Humans,
pubmed-meshheading:15093542-I-kappa B Proteins,
pubmed-meshheading:15093542-Lymphoma, Large-Cell, Anaplastic,
pubmed-meshheading:15093542-NF-kappa B,
pubmed-meshheading:15093542-Oncogene Proteins, Fusion,
pubmed-meshheading:15093542-Phenotype,
pubmed-meshheading:15093542-Phosphorylation,
pubmed-meshheading:15093542-Protein Binding,
pubmed-meshheading:15093542-Protein-Tyrosine Kinases,
pubmed-meshheading:15093542-Proteins,
pubmed-meshheading:15093542-Signal Transduction,
pubmed-meshheading:15093542-TNF Receptor-Associated Factor 2,
pubmed-meshheading:15093542-Tyrosine
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
The NPM-ALK oncoprotein abrogates CD30 signaling and constitutive NF-kappaB activation in anaplastic large cell lymphoma.
|
|
pubmed:affiliation |
Fourth Department of Internal Medicine, Faculty of Medicine, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 228-8555, Japan.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
