Hostname: page-component-78c5997874-g7gxr Total loading time: 0 Render date: 2024-11-10T16:03:50.917Z Has data issue: false hasContentIssue false

Structural Characterization of Iron in Human Spleen

Published online by Cambridge University Press:  15 March 2011

Martin Kopani
Affiliation:
Institute of Pathology, Faculty of Medicine, Comenius University, Sasinkova 4, 811 08 Bratislava, Slovakia
Marcel Miglierini
Affiliation:
Slovak University of Technology, Faculty of Electrical Engineering and Information Technology, Department of Nuclear Physics, 812 19 Bratislava, Slovakia
Adriana Lancok
Affiliation:
Institute of Inorganic Chemistry, Academy of Science, 25068 Husinec4Rez, Czech Republic
Stanislav Jurecka
Affiliation:
Department of Engineering Fundamentals, Faculty of Electrical Engineering, University of Zilina, 031 01 Liptovsky Mikulas, Slovakia
Julius Dekan
Affiliation:
Slovak University of Technology, Faculty of Electrical Engineering and Information Technology, Department of Nuclear Physics, 812 19 Bratislava, Slovakia
Milan Melnik
Affiliation:
Slovak University of Technology, Faculty of Chemical and Food Technology, Department of Inorganic Chemistry, Radlinskeho 9, 812 37 Bratislava, Slovakia
Vladimir Sisovsky
Affiliation:
Institute of Pathology, Faculty of Medicine, Comenius University, Sasinkova 4, 811 08 Bratislava, Slovakia
Milan Mikula
Affiliation:
Slovak University of Technology, Faculty of Chemical and Food Technology, Department of Graphics Arts Technology and Applied Photochemistry, Radlinskeho 9, 812 37 Bratislava, Slovakia
Jan Manka
Affiliation:
Institute of Measurement Science, Slovak Academy of Science, Dubravska cesta 9, 841 04 Bratislava, Slovakia
Martin Skratek
Affiliation:
Institute of Measurement Science, Slovak Academy of Science, Dubravska cesta 9, 841 04 Bratislava, Slovakia
Ludovit Danihel
Affiliation:
Institute of Pathology, Faculty of Medicine, Comenius University, Sasinkova 4, 811 08 Bratislava, Slovakia
Jan Jakubovsky
Affiliation:
Institute of Pathology, Faculty of Medicine, Comenius University, Sasinkova 4, 811 08 Bratislava, Slovakia
Get access

Abstract

Iron is essential element for fundamental cell functions, catalyst for chemical reaction. Iron can be found in human body mainly in the form of ferritin - 5Fe2O3.9H2O.

57Fe Mössbauer spectrometry, X4ray powder diffraction, (XRD), X4ray fluorescence (XRF), scanning and transmission electron microscopy (TEM) were carried out for investigation of iron oxide particles in human spleens with diagnosis of hemosiderosis, hereditary spherocytosis, and reference sample.

Room temperature Mössbauer spectra of all investigated samples exhibit doublet4like features identified as Fe(III) predominantly in ferrihydrite and haem environments within the tissue. Low temperature Mössbauer effect measurements at 77 K revealed, however, no changes in the magnetic ordering of the investigated samples. A contribution of ferromagnetically split sextets is clearly seen for all investigated samples measured at 5K. Their occurrence indicates that part of the sample is magnetically ordered, i.e. below the blocking temperature of a superparamagnetic behaviour. The ratio of relative contents of doublet to sextet components suggests differences in the size of ferritin cores in the investigated samples. The hemosiderosis sample exhibits the largest ferritin core which, in turn, stores the highest amount of Fe and thus triggers this disease.

Additional structural characterization is obtained from powder XRD and XRF measurements. XRF results show presence of different chemical elements such as iron, sulphur, phosporus, chlorine, zinc, chromium, and bromine. TEM investigation reveals iron accumulation in macrophages of the human spleen. The size of the particles is around 5 μm.

The amount of chemical elements and pH in surrounding environments can influence iron oxidation status and may cause transformation of biogenic to abiogenic (toxic) character of ferritin.

Type
Research Article
Copyright
Copyright © Materials Research Society 2009

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Kopani, M., Weis, M., Jakubovsky, J., Dekan, J., Analysis of Human Spleen Contamination. in Solids at the Biological Interface, ed. Ferguson, V.L., Zhang, J.X.-J., Stoldt, C., Frick, C.P. (Mater. Res. Soc. Symp. Proc. Vol. 1063E, Warrendale, PA, 2007), 1063-OO09-13Google Scholar
2. Saenz, J.J, Garcia, N., Grutter, P., Meyer, P., Heinzelmann, H., Wiesendanger, R., Rosenthaler, L., Hidber, H.R, Guntherodt, H.J, J. Appl. Phys. 62, 4293 (1987)Google Scholar
3. Wadas, A., Grütter, P., Phys. Rew. B 39, 12013 (1988)Google Scholar
4. Chhabra, A., Jensen, R.V., Phys. Rev. Lett. 62, 1327 (1989)Google Scholar
5. Mandelbrot, B.B..: A Fractal's Lacunarity, and how it can be Tuned and Measured. Fractals in biology and medicine eds Nonnenmacher, T.F., Losa, G.A., Weibel, E.R.. Basel and Boston: Birkhäuser Verlag, 1994 Google Scholar
6. Castleman, K.R: Digital image processing. Prentice-Hall, New Jersey, 1996.Google Scholar
7. Hromec, A., J. Jakubovsky. Cesk. Physiol. 32, 438443 (1983)Google Scholar
8. Jang, J.H., Dempsey, B.A., Catchen, G.L., Burgos, W.D., Colloids Surf. 221, 5568 (2003)Google Scholar
9. Meyrick, D., Webb, J., Cole, C., Inorg. Chim. Acta 339, 481487 (2002)Google Scholar
10. Pierre, T. G. St., Pollard, R. K., Dickson, D. P. E, Ward, R. J., Peters, T. J., Biochim. Biophys. Acta 952, 158163 (1988)Google Scholar