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dc.contributor.authorGriffiths, Stephen D
dc.contributor.authorBurthem, John
dc.contributor.authorUnwin, Richard D
dc.contributor.authorHolyoake, Tessa L
dc.contributor.authorMelo, Junia V
dc.contributor.authorLucas, Guy S
dc.contributor.authorWhetton, Anthony D
dc.date.accessioned2009-06-15T11:47:58Z
dc.date.available2009-06-15T11:47:58Z
dc.date.issued2007-06
dc.identifier.citationThe use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia. 2007, 36 (2):81-9 Mol. Biotechnol.en
dc.identifier.issn1073-6085
dc.identifier.pmid17914187
dc.identifier.doi10.1007/s12033-007-0005-5
dc.identifier.urihttp://hdl.handle.net/10541/70439
dc.description.abstractChronic Myeloid Leukemia (CML) is a hematopoietic stem cell disease, associated with a t(9, 22) chromosomal translocation leading to formation of the BCR/ABL chimeric protein, which has an intrinsic tyrosine kinase activity. Recently, the BCR/ABL tyrosine kinase inhibitor imatinib mesylate (imatinib) has been successfully used clinically, although, disease relapse can still occur. The precise detail of the mechanism by which CML cells respond to imatinib is still unclear. We therefore systematically examined the effects of imatinib on the primitive CML cell proteome, having first established that the drug inhibits proliferation and induces increased apoptosis and differentiation. To define imatinib-induced effects on the CML proteome, we employed isobaric tag peptide labeling (iTRAQ) coupled to two-dimensional liquid chromatography/tandem mass spectrometry. Given the limited clinical material available, the isobaric tag approach identified a large population of proteins and provided relative quantification on four samples at once. Novel consequences of the action of imatinib were identified using this mass spectrometric approach. DEAD-box protein 3, heat shock protein 105 kDa, and peroxiredoxin-3 were identified as potential protein markers for response to imatinib.
dc.language.isoenen
dc.subjectLeukaemiaen
dc.subjectTumour Cellsen
dc.subject.meshAntineoplastic Agents
dc.subject.meshApoptosis
dc.subject.meshCell Differentiation
dc.subject.meshCell Proliferation
dc.subject.meshChromatography, Liquid
dc.subject.meshDEAD-box RNA Helicases
dc.subject.meshHSP110 Heat-Shock Proteins
dc.subject.meshHematopoietic Stem Cells
dc.subject.meshHumans
dc.subject.meshLeukemia, Myelogenous, Chronic, BCR-ABL Positive
dc.subject.meshPeptides
dc.subject.meshPeroxidases
dc.subject.meshPeroxiredoxins
dc.subject.meshPiperazines
dc.subject.meshProtein Kinase Inhibitors
dc.subject.meshProteome
dc.subject.meshProteomics
dc.subject.meshPyrimidines
dc.subject.meshTandem Mass Spectrometry
dc.subject.meshTumor Cells, Cultured
dc.titleThe use of isobaric tag peptide labeling (iTRAQ) and mass spectrometry to examine rare, primitive hematopoietic cells from patients with chronic myeloid leukemia.en
dc.typeArticleen
dc.contributor.departmentDivision of Cancer Studies, Faculty of Medical and Human Sciences, Christie Hospital, University of Manchester, Wilmslow Road, Manchester M20 9BX, UK.en
dc.identifier.journalMolecular Biotechnologyen
html.description.abstractChronic Myeloid Leukemia (CML) is a hematopoietic stem cell disease, associated with a t(9, 22) chromosomal translocation leading to formation of the BCR/ABL chimeric protein, which has an intrinsic tyrosine kinase activity. Recently, the BCR/ABL tyrosine kinase inhibitor imatinib mesylate (imatinib) has been successfully used clinically, although, disease relapse can still occur. The precise detail of the mechanism by which CML cells respond to imatinib is still unclear. We therefore systematically examined the effects of imatinib on the primitive CML cell proteome, having first established that the drug inhibits proliferation and induces increased apoptosis and differentiation. To define imatinib-induced effects on the CML proteome, we employed isobaric tag peptide labeling (iTRAQ) coupled to two-dimensional liquid chromatography/tandem mass spectrometry. Given the limited clinical material available, the isobaric tag approach identified a large population of proteins and provided relative quantification on four samples at once. Novel consequences of the action of imatinib were identified using this mass spectrometric approach. DEAD-box protein 3, heat shock protein 105 kDa, and peroxiredoxin-3 were identified as potential protein markers for response to imatinib.


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