Source:http://linkedlifedata.com/resource/pubmed/id/10706082
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2000-3-20
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| pubmed:abstractText |
Anaplastic lymphoma kinase (ALK)-positive lymphomas ("ALKomas") constitute a distinct molecular and clinicopathological entity within the heterogeneous group of CD30-positive large cell lymphomas. In 80-85% of cases tumor cells express a Mr 80,000 hybrid protein comprising the nucleolar phosphoprotein nucleophosmin (NPM) and the ALK. We report here the cloning and expression of a novel ALK-fusion protein from an ALK-positive lymphoma. This case was selected for molecular investigation because of (a) the absence of NPM-ALK transcripts; (b) the atypical staining patterns for ALK (cytoplasm-restricted) and for NPM (nucleus-restricted); and (c) the presence of a Mr 96,000 ALK-protein differing in size from NPM-ALK. Nucleotide sequence analysis of ALK transcripts isolated by 5'-rapid amplification of cDNA ends revealed a chimeric mRNA corresponding to an ATIC-ALK in-frame fusion. ATIC is a bifunctional enzyme (5-aminoimidazole-4-carboxamide ribonucleotide transformylase and IMP cyclohydrolase enzymatic activities) that catalyzes the penultimate and final enzymatic activities of the purine nucleotide synthesis pathway. Expression of full-length ATIC-ALK cDNA in mouse fibroblasts revealed that the fusion protein (a) possesses constitutive tyrosine kinase activity; (b) forms stable complexes with the signaling proteins Grb2 and Shc; (c) induces tyrosine-phosphorylation of Shc; and (d) provokes oncogenic transformation. These findings point to fusion with ATIC as an alternative mechanism of ALK activation.
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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/IMP cyclohydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotide Deaminases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/anaplastic lymphoma kinase,
http://linkedlifedata.com/resource/pubmed/chemical/nucleophosmin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0008-5472
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
60
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
793-8
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| pubmed:dateRevised |
2011-11-17
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| pubmed:meshHeading |
pubmed-meshheading:10706082-3T3 Cells,
pubmed-meshheading:10706082-Adolescent,
pubmed-meshheading:10706082-Amino Acid Sequence,
pubmed-meshheading:10706082-Animals,
pubmed-meshheading:10706082-Base Sequence,
pubmed-meshheading:10706082-Cell Transformation, Neoplastic,
pubmed-meshheading:10706082-Cloning, Molecular,
pubmed-meshheading:10706082-Humans,
pubmed-meshheading:10706082-Lymphoma, Large B-Cell, Diffuse,
pubmed-meshheading:10706082-Male,
pubmed-meshheading:10706082-Mice,
pubmed-meshheading:10706082-Molecular Sequence Data,
pubmed-meshheading:10706082-Nuclear Proteins,
pubmed-meshheading:10706082-Nucleotide Deaminases,
pubmed-meshheading:10706082-Phosphorylation,
pubmed-meshheading:10706082-Protein-Tyrosine Kinases,
pubmed-meshheading:10706082-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:10706082-Recombinant Fusion Proteins
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| pubmed:year |
2000
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| pubmed:articleTitle |
A new variant anaplastic lymphoma kinase (ALK)-fusion protein (ATIC-ALK) in a case of ALK-positive anaplastic large cell lymphoma.
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| pubmed:affiliation |
Department of Experimental Oncology, Istituto Europeo di Oncologia, Milan, Italy.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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