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Title
Iron speciation in human cancer cells by K-edge Total Reflection X-ray Fluorescence-X-ray Absorption Near Edge Structure
AuthorPolgári, Zsófia ; Meirer, Florian ; Sasamori, Sato ; Ingerle, Dieter ; Pepponi, Giancarlo ; Streli, Christina In der Gemeinsamen Normdatei der DNB nachschlagen ; Rickers, Karen ; Réti, Andrea ; Budai, Barna ; Szoboszlai, Norbert ; Záray, Gyula
Published in
Spectrochimica Acta Part B: Atomic Spectroscopy, 2011, Vol. 66, Issue 3-4, page 274-279
Published2011
Edition
Accepted version
LanguageEnglish
Document typeJournal Article
Keywords (EN)Cancer cell / Iron / TXRF / XANES
URNurn:nbn:at:at-ubtuw:3-1442 Persistent Identifier (URN)
DOI10.1016/j.sab.2011.03.011 
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Iron speciation in human cancer cells by K-edge Total Reflection X-ray Fluorescence-X-ray Absorption Near Edge Structure [2.53 mb]
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Abstract (English)

X-ray absorption near edge structure (XANES) analysis in combination with synchrotron radiation induced total reflection X-ray fluorescence (SR-TXRF) acquisition was used to determine the oxidation state of Fe in human cancer cells and simultaneously their elemental composition by applying a simple sample preparation procedure consisting of pipetting the cell suspension onto the quartz reflectors.

XANES spectra of several inorganic and organic iron compounds were recorded and compared to that of different cell lines. The XANES spectra of cells, independently from the phase of cell growth and cell type were very similar to that of ferritin, the main Fe store within the cell. The spectra obtained after CoCl2 or NiCl2 treatment, which could mimic a hypoxic state of cells, did not differ noticeably from that of the ferritin standard. After 5-fluorouracil administration, which could also induce an oxidative-stress in cells, the absorption edge position was shifted toward higher energies representing a higher oxidation state of Fe. Intense treatment with antimycin A, which inhibits electron transfer in the respiratory chain, resulted in minor changes in the spectrum, resembling rather the N-donor Fe-,′-dipyridyl complex at the oxidation energy of Fe(III), than ferritin. The incorporation of Co and Ni in the cells was followed by SR-TXRF measurements.

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