Source:http://linkedlifedata.com/resource/pubmed/id/11502748
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
42
|
| pubmed:dateCreated |
2001-10-15
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| pubmed:abstractText |
The Dbl homology (DH) domain of BCR in P210BCR-ABL (P210/WT) has been thought to have a negative effect on the activation of BCR-ABL because P185BCR-ABL, in which this region is physically deleted, has stronger biochemical and biological activities. To study the role of the DH domain of BCR in the background of P210/WT, the region was replaced with homologous sequences derived from Dbl (P210/Dbl) or CDC24 (P210/CDC24) or with irrelevant sequences from LacZ (P210/LacZ) or luciferase (P210/Luci). Surprisingly, the abilities to transform Rat1 cells or mouse bone marrow cells and induce growth factor independence in interleukin 3-dependent mouse Ba/F3 cells were retained only in P210/Dbl. However, even P210/Dbl could not achieve the wild type level of surviving potential against genotoxins in Rat1 cells and in Ba/F3 cells. Activation of Akt correlated with the biological changes in Rat1 cells but did not correlate with the biological changes in Ba/F3 cells. The DH domain was not tyrosine-phosphorylated in vitro, nor could we find any differences in peptide mapping between in vitro phosphorylated P210/WT and P210/Dbl. Although functions of the DH domain remain to be discovered, we propose that the DH domain makes positive contributions to P210BCR-ABL.
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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/Fusion Proteins, bcr-abl,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Mcf2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
19
|
| pubmed:volume |
276
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
39462-8
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11502748-Animals,
pubmed-meshheading:11502748-Apoptosis,
pubmed-meshheading:11502748-Bone Marrow Cells,
pubmed-meshheading:11502748-Cell Line,
pubmed-meshheading:11502748-Fusion Proteins, bcr-abl,
pubmed-meshheading:11502748-Gene Deletion,
pubmed-meshheading:11502748-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:11502748-Lac Operon,
pubmed-meshheading:11502748-Luciferases,
pubmed-meshheading:11502748-Mice,
pubmed-meshheading:11502748-Mutation,
pubmed-meshheading:11502748-Philadelphia Chromosome,
pubmed-meshheading:11502748-Phosphorylation,
pubmed-meshheading:11502748-Protein Binding,
pubmed-meshheading:11502748-Protein Structure, Tertiary,
pubmed-meshheading:11502748-Proto-Oncogene Proteins,
pubmed-meshheading:11502748-Rats,
pubmed-meshheading:11502748-Time Factors,
pubmed-meshheading:11502748-Transformation, Genetic,
pubmed-meshheading:11502748-Tyrosine
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| pubmed:year |
2001
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| pubmed:articleTitle |
The Dbl homology domain of BCR is not a simple spacer in P210BCR-ABL of the Philadelphia chromosome.
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| pubmed:affiliation |
Department of Genetics, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-0071, Japan.
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| pubmed:publicationType |
Journal Article
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