NDLI: Biophysical and genetic analysis of iron partitioning and ferritin function in Drosophila melanogaster

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Metallomics Vol - 5 Issue - 7

Metallomics Vol - 5 Issue - 6

Metallomics Vol - 5 Issue - 5

Metallomics Vol - 5 Issue - 4

Metallomics Vol - 5 Issue - 3

Metallomics Vol - 5 Issue - 2

Biophysical and genetic analysis of iron partitioning and ferritin function in Drosophila melanogaster

Content Provider	Royal Society of Chemistry (RSC)
Author	irlis, Fanis Lázaro, Francisco J. Gambis, Alexis Mollereau, Bertrand Gutiérrez, Lucía Nield, Jon Zubow, Kristina
Copyright Year	2013
Abstract	Metals have vital functions as prosthetic groups in enzymes, but in labile form they can propagate oxidative stress. The primary function of ferritin is to store bioavailable iron in the form of ferrihydrite. In animals, ferritin is also used to traffic and recycle iron, and to modulate intestinal iron absorption. However, the effect of ferritin accumulation on cellular iron bioavailability remains poorly understood. Moreover, putative in vivo interactions of ferritin with other metal ions have been proposed, but their physiological relevance remains unclear. Here, heterozygous mutant and overexpression ferritin strains of Drosophila melanogaster were subjected to dietary iron manipulations to study the dynamics of iron partition between ferritin and other proteins. Quantitative magnetic analysis of whole fly samples indicated that iron loading of the ferritin core varied in the different genotypes. Total paramagnetic iron content, a likely correlate of bioavailable iron, was reduced in flies overexpressing ferritin when compared with control white flies. Further, three-dimensional maps of the ferritin protein shell and iron core were obtained from single particle transmission electron microscopy imaging and confirmed the similarity between Drosophila and Trichoplusia ferritin structures. Purified Drosophila ferritin also contained small amounts of zinc and manganese. Flies that overexpressed ferritin accumulated in their bodies half the amount of manganese compared to their respective controls. Our results indicate that ferritin may be involved in the homeostasis of other divalent metals, besides iron, and that overexpression of ferritin, sometimes employed to rescue neurodegenerative models of disease, serves to limit divalent metal bio-availability in cells.
Starting Page	997
Ending Page	1005
Page Count	9
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	5
Issue Number	8
Journal	Metallomics
DOI	10.1039/c3mt00118k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Oxidative stress Ferrihydrite Drosophila Ferritin Paramagnetism Homeostasis Bioavailability Protein Zinc Zygosity Transmission electron microscopy Mutation Drosophila melanogaster Manganese
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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