| pubmed-article:10849448 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10849448 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:10849448 | lifeskim:mentions | umls-concept:C0023470 | lld:lifeskim |
| pubmed-article:10849448 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:10849448 | lifeskim:mentions | umls-concept:C0079189 | lld:lifeskim |
| pubmed-article:10849448 | lifeskim:mentions | umls-concept:C0085862 | lld:lifeskim |
| pubmed-article:10849448 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:10849448 | pubmed:dateCreated | 2000-7-20 | lld:pubmed |
| pubmed-article:10849448 | pubmed:abstractText | Bcr-Abl is the constitutively active protein-tyrosine kinase expressed as a result of the Philadelphia translocation in chronic myelogenous leukemia. Bcr-Abl is coupled to many of the same signaling pathways normally regulated by hematopoietic cytokines. Recent work shows that Hck, a member of the Src tyrosine kinase family with myeloid-restricted expression, associates with and is activated by Bcr-Abl. Here we investigated the mechanism of Hck interaction with Bcr-Abl and the requirement for Hck activation in Bcr-Abl transformation signaling. Binding studies demonstrated that the Hck SH3 and SH2 domains are sufficient for interaction with Bcr-Abl in vitro. Hck binding localizes to the Abl SH2, SH3, and kinase domains as well as the distal portion of the C-terminal tail. To address the requirement for endogenous Src family kinase activation in Bcr-Abl signaling, a kinase-defective mutant of Hck was stably expressed in the cytokine-dependent myeloid leukemia cell line DAGM. Kinase-defective Hck dramatically suppressed Bcr-Abl-induced outgrowth of these cells in the absence of cytokine compared with a control cell line expressing beta-galactosidase. In contrast, kinase-defective Hck did not affect cell proliferation in response to interleukin-3, suggesting that the effect is specific for Bcr-Abl. These data show that Hck interacts with Bcr-Abl through a complex mechanism involving kinase-dependent and -independent components and that interaction with Hck or other Src family members is essential for transformation signaling by Bcr-Abl. | lld:pubmed |
| pubmed-article:10849448 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10849448 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10849448 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10849448 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10849448 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10849448 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10849448 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10849448 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10849448 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10849448 | pubmed:author | pubmed-author:WilsonM BMB | lld:pubmed |
| pubmed-article:10849448 | pubmed:author | pubmed-author:SmithgallT... | lld:pubmed |
| pubmed-article:10849448 | pubmed:author | pubmed-author:LionbergerJ... | lld:pubmed |
| pubmed-article:10849448 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10849448 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:10849448 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10849448 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10849448 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10849448 | pubmed:pagination | 18581-5 | lld:pubmed |
| pubmed-article:10849448 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10849448 | pubmed:meshHeading | pubmed-meshheading:10849448... | lld:pubmed |
| pubmed-article:10849448 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10849448 | pubmed:articleTitle | Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck. | lld:pubmed |
| pubmed-article:10849448 | pubmed:affiliation | Department of Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA. | lld:pubmed |
| pubmed-article:10849448 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10849448 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10849448 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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