title: Studies on haemosiderin and ferritin from iron-loaded rat liver.
abstract: Haemosiderin has been isolated from siderosomes and ferritin from the cytosol of livers of rats iron-loaded by intraperitoneal injections of iron-dextran. Siderosomal haermosiderin, like ferritin, was shown by electron diffraction to contain iron mainly in the form of small particles of ferrihydrite (5Fe2O3.9H2O), with average particle diameter of 5.36 +/- 1.31 nm (SD), less than that of ferritin iron-cores (6.14 +/- 1.18 nm). Mössbauer spectra of both iron-storage complexes are also similar, except that the blocking temperature, TB, for haemosiderin (23 K) is lower than that of ferritin (35 K). These values are consistent with their differences in particle volumes assuming identical magnetic anisotropy constants. Measurements of P/Fe ratios by electron probe microanalysis showed the presence of phosphorus in rat liver haemosiderin, but much of it was lost on extensive dialysis. The presence of peptides reacting with anti-ferritin antisera and the similarities in the structures of their iron components are consistent with the view that rat liver haemosiderin arises by degradation of ferritin polypeptides, but its peptide pattern is different from that found in human beta-thalassaemia haemosiderin. The blocking temperature, 35 K, for rat liver ferritin is near to that reported, 40 K, for human beta-thalassaemia spleen ferritin. However, the haemosiderin isolated from this tissue, in contrast to that from rat liver, had a TB higher than that of ferritin. The iron availability of haemosiderins from rat liver and human beta-thalassaemic spleen to a hydroxypyridinone chelator also differed. That from rat liver was equal to or greater, and that from human spleen was markedly less, than the iron availability from either of the associated ferritins, which were equivalent. The differences in properties of the two types of haemosiderin may reflect their origins from primary or secondary iron overload and differences in the duration of the overload.
authors.affiliation: Department of Biochemistry, University of Sheffield, UK.
authors.forename: S C
authors.initials: SC
authors.lastname: Andrews
authors.forename: M C
authors.initials: MC
authors.lastname: Brady
authors.forename: A
authors.initials: A
authors.lastname: Treffry
authors.forename: J M
authors.initials: JM
authors.lastname: Williams
authors.forename: S
authors.initials: S
authors.lastname: Mann
authors.forename: M I
authors.initials: MI
authors.lastname: Cleton
authors.forename: W
authors.initials: W
authors.lastname: de Bruijn
authors.forename: P M
authors.initials: PM
authors.lastname: Harrison
mesh_terms: D000818:Animals; D004577:Electron Probe Microanalysis; D005260:Female; D005293:Ferritins / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D006485:Hemosiderin / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D007120:Immunochemistry; D007501:Iron / Q000008:administration & dosage / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D010446:Peptide Fragments / Q000276:immunology / Q000302:isolation & purification; D010758:Phosphorus / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D015204:Spectroscopy, Mossbauer
chemical_list: D010446:Peptide Fragments; D010758:Phosphorus; D005293:Ferritins; D006485:Hemosiderin; D007501:Iron