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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
1996-8-20
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pubmed:abstractText |
Bcr-Abl oncoproteins are responsible for the pathogenesis of human leukemias with a reciprocal chromosome translocation t(9;22). The amino-terminal Bcr sequence has a potential to form a homotetramer (tetramer domain), and destructions of the tetramer domain cause a complete loss of biological activities in Bcr-Abl. Here we show that Bcr-Abl in which the tetramer domain is replaced with glutathione S-transferase (GST) with a dimerizing ability (GST/Bcr-Abl-(Delta1-160)) can no longer induce an interleukin-3 (IL-3) independence in Ba/F3 cells or transform mouse bone marrow cells but still retains by 30-40% the ability to transform Rat1 cells. Compared with the wild type Bcr-Abl, autophosphorylation of GST/Bcr-Abl-(Delta1-160) in vivo was reduced by more than 50%. The Grb-2 binding to GST/Bcr-Abl-(Delta1-160) was 50% reduced in Rat1 cells and undetectable in Ba/F3 cells. In Rat1 cells expressing GST/Bcr-Abl-(Delta1-160), phosphotyrosine contents of p62 and Shc were 70% decreased.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Fusion Proteins, bcr-abl,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Grb2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Grb2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15353-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8663064-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:8663064-Animals,
pubmed-meshheading:8663064-Bone Marrow Cells,
pubmed-meshheading:8663064-Cell Transformation, Neoplastic,
pubmed-meshheading:8663064-Cells, Cultured,
pubmed-meshheading:8663064-Fusion Proteins, bcr-abl,
pubmed-meshheading:8663064-GRB2 Adaptor Protein,
pubmed-meshheading:8663064-Glutathione Transferase,
pubmed-meshheading:8663064-Macromolecular Substances,
pubmed-meshheading:8663064-Mice,
pubmed-meshheading:8663064-Phosphotyrosine,
pubmed-meshheading:8663064-Protein Binding,
pubmed-meshheading:8663064-Protein-Tyrosine Kinases,
pubmed-meshheading:8663064-Proteins,
pubmed-meshheading:8663064-Rats,
pubmed-meshheading:8663064-Recombinant Fusion Proteins,
pubmed-meshheading:8663064-Structure-Activity Relationship
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pubmed:year |
1996
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pubmed:articleTitle |
The dimerization property of glutathione S-transferase partially reactivates Bcr-Abl lacking the oligomerization domain.
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pubmed:affiliation |
Department of Genetics, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan.
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pubmed:publicationType |
Journal Article
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