Journal article
Quantitation and localization of intracellular redox active metals by X-ray fluorescence microscopy in cortical neurons derived from APP and APLP2 knockout tissue
GD Ciccotosto, SA James, M Altissimo, D Paterson, S Vogt, B Lai, MD De Jonge, DL Howard, AI Bush, R Cappai
Metallomics | ROYAL SOC CHEMISTRY | Published : 2014
DOI: 10.1039/c4mt00176a
Abstract
The amyloid precursor protein (APP) gene family includes APP and the amyloid precursor-like proteins, APLP1 and APLP2. These proteins contain metal binding sites for copper, zinc and iron and are known to have physiological roles in modulating the metal homeostasis in brain cells. Here we report the application of X-ray fluorescence microscopy (XFM) to investigate the subcellular distribution patterns of the metal ions Cu, Zn, Fe, and Ca in individual neurons derived from APP and APLP2 knockout mice brains to further define their role in metal homeostasis. These studies add to the growing body of data that the APP family of proteins are metalloproteins that have shared as well as distinct ef..
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Grants
Awarded by Argonne National Laboratory
Awarded by Australian Synchrotron Research Fund
Funding Acknowledgements
This work was supported by funds from the Australian Research Council, the Australian National Health and Medical Research Council and Operational Infrastructure Support Victorian State Government. This research used resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Access was made possible through the financial assistance of the Australian Synchrotron Research Fund (proposal AS_IA083/APS10858). We acknowledge travel funding provided by the International Synchrotron Access Program managed by the Australian Synchrotron and funded by the Australian Government. Part of this research was undertaken on the XFM beamline at the Australian Synchrotron, Victoria, Australia.