Iron-binding proteins

Acta Paediatrica Scandinavica. Supplement
J H Brock

Abstract

The structure and properties of the iron-binding proteins transferrin, lactoferrin and transferrin are reviewed. Transferrin and lactoferrin are structurally similar, consisting of a single polypeptide chain and reversibly binding two iron atoms per molecule. Transferrin is found mainly in serum, whereas lactoferrin is found in neutrophils and in external secretions. Transferrin functions mainly as a donor of iron to cells, but there is no established iron-transport role for lactoferrin. Both these proteins may have antimicrobial activity as a result of their ability to sequester iron. Lactoferrin may act principally as a scavenger of iron in conditions where transferrin may not bind iron well, e.g. at low pH. Ferritin is a multisubunit protein capable of binding up to 4,000 iron atoms and serves principally as an iron-storage protein, though it may also serve to detoxify iron. In iron-rich tissues ferritin is largely degraded and the iron is converted to haemosiderin.

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Citations

Jan 1, 1989·Acta Paediatrica Scandinavica. Supplement·P R Flanagan
Feb 1, 1997·Environmental Health Perspectives·G A LeBlanc, L J Bain
Nov 25, 2003·Journal of Oral Pathology & Medicine : Official Publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology·Toyohiro TanidaTokio Osaki
Sep 1, 2020·Immunity, Inflammation and Disease·Damini TewariHelen Collins
Sep 1, 1994·Acta Paediatrica. Supplement·R Chierici, V Vigi
May 16, 2006·Immunobiology·Sek Tong OngJeak Ling Ding

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