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Analysis of iron-containing compounds in different compartments of the rat liver after iron loading
Authors:Patricia L Ringeling  Maud I Cleton  Marja I E Huijskes-Heins  Marionne J E Seip  Wim C de Bruijn  Henk G van Eijk
Institution:(1) Departments of Chemical Pathology, Erasmus University Rotterdam, P. O. Box 1738, NL-3000 DR Rotterdam, The Netherlands;(2) Departments of Pathological Atonomy, AEM Unit, Erasmus University Rotterdam, P. O. Box 1738, NL-3000 DR Rotterdam, The Netherlands
Abstract:Summary The livers of iron-loaded rats were fractionated and a cytosolic fraction, a lysosomal fraction, a siderosomal fraction and haemosiderin were obtained. All iron-containing compounds from these fractions were isolated and their morphology, Fe/P ratios, iron core diameter and peptide content were compared. The cytosolic fraction contained ferritin (CF) and a slower sedimenting, light ferritin (CLF). The lysosomal fraction also contained ferritin (LF) and a slower sedimenting light ferritin (LLF). The siderosomal fraction contained ferritin (SF), a faster sedimenting non-ferritin iron compound (SIC) and haemosiderin (HS). SIC and HS did not resemble ferritin as much as the other products did, but were found to be water-insoluble aggregates. The Fe/P ratios of CF and CLF were lower than the Fe/P ratios of LF and LLF and these in turn had lower Fe/P ratios than SF, SIC and HS. The iron core diameter of the cytosolic ferritin was increased after lysosomal uptake. The iron core diameters of the siderosomal products were smaller. CLF, CF, LF, LLF and SF contained one kind of subunit of approximately 20.5 kDa. SIC and HS contained other peptides in addition to the 20.5-kDa subunit. The results indicate that storage of ferritin molecules is not limited to the cytosolic compartment, but is also the case in the lysosomes. Extensive degradation of the ferritin molecule seems to be confined to the siderosomes.
Keywords:Electron spectroscopy  Ferritin  Haemosiderin  Iron-loaded rat  Morphometry
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