Proceedings of the Nutrition Society (1995), 54, 509-517
Riboflavin-iron interactions with particular emphasis on the gastrointestinal tract
BY HILARY J. POWERS
The University Department of Paediatrics, Shefield Children’s Hospital, Shefield SIO 2TH
Riboflavin-responsive anaemia in man was described as early as the 1950s (Foy & Kondi, 1953, 1958). The characteristic features included an erythroid hypoplasia and reticulocytopenia. Xanthurenic aciduria, indicative of abnormal tryptophan metabolism, was also reported and suggested that some of the effects of riboflavin deficiency may be secondary to interference with pyridoxine metabolism (Rasmussen et al. 1979). Riboflavin depletion-repletion studies demonstrated that plasma Fe clearance, also, might be impaired in riboflavin deficiency in humans (Lane et al. 1964).
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FERRITIN-IRON MOBILIZATION Ferritin is a predominantly intracellular Fe-storage protein. Fe is retained in the protein shell of ferritin in the oxidized form, Fe3+, and requires reduction in order to be released (Frieden & Osaki, 1974). Considerable interest has been shown in the likely physiological mechanism whereby ferritin-Fe could be mobilized; various biological reductants, such as ascorbic acid and glutathione, can reduce ferritin-Fe to Fe2+ but at rates that are unlikely to be of any physiological significance. Reduced flavins on the other hand are capable of reducing ferritin-Fe in vitro rapidly and quantitatively (Sirivech et al. 1974).