Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5620
Title: Macromolecular changes in nilotinib resistant k562 cells; An in vitro study by fourier transform infrared spectroscopy
Authors: Ceylan, Çağatay
Camgöz, Aylin
Baran, Yusuf
Ceylan, Çağatay
Camgöz, Aylin
Baran, Yusuf
Izmir Institute of Technology. Food Engineering
Keywords: Nilotinib
Tyrosine kinase inhibitor resistance
Chronic myeloid leukemia
Fourier transform infrared spectroscopy
Triacylglycerol
Issue Date: Aug-2012
Publisher: SAGE Publications Inc.
Source: Ceylan, Ç, Camgöz, A. and Baran, Y. (2012). Macromolecular changes in nilotinib resistant k562 cells; An in vitro study by fourier transform infrared spectroscopy. Technology in Cancer Research and Treatment, 11(4), 333-344. doi:10.7785/tcrt.2012.500281
Abstract: Nilotinib is a second generation tyrosine kinase inhibitor which is used in both first and second line treatment of chronic myeloid leukemia (CML). In the present work, the effects of nilotinib resistance on K562 cells were investigated at the molecular level using Fourier transform infrared (FT-IR) spectroscopy. Human K562 CML cells were exposed to step-wise increasing concentrations of nilotinib, and sub-clones of K562 cells resistant to 50 nM nilotinib were generated and referred to as K562/NIL-50 cells. Antiproliferative effects of nilotinib were determined by XTT cell proliferation assay. Changes in macromolecules in parental and resistant cells were studied by FT-IR spectroscopy. Nilotinib resistance caused significant changes which indicated increases in the level of glycogen and membrane/lipid order. The amount of unsaturated lipids increased in the nilotinib resistant cells indicating lipid peroxidation. The total amount of lipids did not change significantly but the relative proportion of cholesterol and triglycerides altered considerably. Moreover, the transcriptional status decreased but metabolic turn-over increased as revealed by the FT-IR spectra. In addition, changes in the proteome and structural changes in both proteins and the nucleus were observed in the K562/NIL-50 cells. Protein secondary structural analyses revealed that alpha helix structure and random coil structure decreased, however, anti-parallel beta sheet structure, beta sheet structure and turns structure increased. These results indicate that the FT-IR technique provides a method for analyzing drug resistance related structural changes in leukemia and other cancer types.
URI: http://dx.doi.org/10.7785/tcrt.2012.500281
http://hdl.handle.net/11147/5620
ISSN: 1533-0346
1533-0338
Appears in Collections:Food Engineering / Gıda Mühendisliği
Molecular Biology and Genetics / Moleküler Biyoloji ve Genetik
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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