dc.creatorTraina, Fabíola
dc.creatorCarvalheira, José Barreto C
dc.creatorSaad, Mario J A
dc.creatorCosta, Fernando F
dc.creatorSaad, Sara T O
dc.date2003-Jan
dc.date2015-11-27T12:52:08Z
dc.date2015-11-27T12:52:08Z
dc.date.accessioned2018-03-29T00:57:26Z
dc.date.available2018-03-29T00:57:26Z
dc.identifierFebs Letters. v. 535, n. 1-3, p. 17-22, 2003-Jan.
dc.identifier0014-5793
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/12560071
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195384
dc.identifier12560071
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295617
dc.descriptionIn the present study we used K562 cells to demonstrate that insulin receptor substrate 1 (IRS-1) is expressed and constitutively phosphorylated in BCR-ABL(+) cells. We observed association between BCR-ABL/IRS-1, IRS-1/phosphoinositide 3'-kinase (PI3-kinase), and IRS-1/Grb2 in the K562 cell line. Our findings demonstrate that imatinib treatment resulted in marked attenuation of BCR-ABL/IRS-1 association and of IRS-1-stimulated PI3-kinase activity in K562 cells. We concluded that the IRS-1 protein is involved in the signalling pathway of the BCR-ABL tyrosine kinase.
dc.description535
dc.description17-22
dc.languageeng
dc.relationFebs Letters
dc.relationFEBS Lett.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectBenzamides
dc.subjectBlotting, Western
dc.subjectDose-response Relationship, Drug
dc.subjectEnzyme Activation
dc.subjectEnzyme Inhibitors
dc.subjectFusion Proteins, Bcr-abl
dc.subjectGrb2 Adaptor Protein
dc.subjectHl-60 Cells
dc.subjectHumans
dc.subjectInsulin Receptor Substrate Proteins
dc.subjectK562 Cells
dc.subjectPhosphatidylinositol 3-kinases
dc.subjectPhosphoproteins
dc.subjectPhosphorylation
dc.subjectPiperazines
dc.subjectProtein Binding
dc.subjectProteins
dc.subjectPyrimidines
dc.titleBcr-abl Binds To Irs-1 And Irs-1 Phosphorylation Is Inhibited By Imatinib In K562 Cells.
dc.typeArtículos de revistas


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