Proteome Changes Induced by Imatinib and Novel Imatinib Derivatives in K562 Human Chronic Myeloid Leukemia Cells
| Autor: | Georgios Tsiotis, Katerina Arvaniti, Konstantinos Skobridis, Maria Kinigopoulou, Anastasia Papadioti, Vassiliki Theodorou |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Clinical Biochemistry
lcsh:QR1-502 Pharmacology Biochemistry SILAC Article lcsh:Microbiology Structural Biology chronic myeloid leukemia hemic and lymphatic diseases Medicine kinase inhibitors Molecular Biology neoplasms protein kinases business.industry Myeloid leukemia Imatinib Imatinib mesylate Nilotinib imatinib Proteome business DDX3X Tyrosine kinase medicine.drug K562 cells |
| Zdroj: | Proteomes Volume 2 Issue 3 Pages 363-381 Proteomes, Vol 2, Iss 3, Pp 363-381 (2014) |
| ISSN: | 2227-7382 |
| DOI: | 10.3390/proteomes2030363 |
| Popis: | Imatinib mesylate is the leading compound to treat chronic myeloid leukemia (CML) and other cancers, through its inhibition of Bcr-Abl tyrosine kinases. However, resistance to imatinib develops frequently, particularly in late-stage disease and has necessitated the development of new Bcr-Abl inhibitors. The synthesis of a new series of phenylaminopyrimidines, structurally related to imatinib, showed large interest since the introduction of nilotinib. Here, we compare the protein levels in K562 cells treated with either imatinib or with novel imatinib derivates. Our results revealed that among the 986 quantified proteins, 35 had significantly altered levels of expression by imatinib or its derivates. In a second series of experiments, we directly compared the proteomes of imatinib treated K562 cells with those K562 cells treated with any of the four imatinib derivates. More than 1029 protein were quantified, 80 of which had altered levels of expression. Both experiments pointed to changes in the expression of the ATP-dependent RNA helicase DDX3X and of two mitochondrial coiled-coil-helix-coiled-coil-helix domain-containing proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|