Structural specificity of haemosiderin iron cores in iron-overload diseases

• Published in: FEBS letters Vol. 234; no. 1; pp. 69 - 72
• Main Authors: Mann, S., Wade, V.J., Dickson, D.P.E., Reid, N.M.K., Ward, R.J., O'Connell, M., Peters, T.J.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 04.07.1988; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Crystallization; Dialysis; Electrophoresis, Polyacrylamide Gel; Ferric Compounds; Ferritins - analysis; Fundamental and applied biological sciences. Psychology; hemochromatosis; Hemochromatosis - metabolism; Hemosiderin; Hemosiderin - analysis; Humans; Iron - analysis; Iron - metabolism; Iron-core structure; Iron-overload; Liver - analysis; Metalloproteins; Microscopy, Electron; Other metalloproteins; Oxalates; Oxalic Acid; Proteins; Proteins - analysis; Solubility; Spectrometry, Gamma; Spleen - analysis; Hemosiderin; Iron-core structure; Iron-overload; Human; Ferroprotein; Chemical coordination; Hemochromatosis; Transmission electron microscopy; Ferritin; Iron
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(88)81305-X

Haemosiderin iron cores isolated from patients with secondary haemochromatosis have a goethite-like (α-FeOOH) crystal structure whereas those from patients with primary haemochromatosis are amorphous Fe (III) oxide. Haemosiderin cores isolated from normal human spleen are crystalline ferrihydrite (5Fe 2O 3·9H 2O). The disease-specific structures are significantly different from the ferrihydrite structure of associated ferritin cores. The results are important in understanding the biological processing of iron in pathological states and in the clinical treatment of iron-overload diseases.