Startseite Medizin Serum pro-hepcidin concentrations and their responses to oral iron supplementation in healthy subjects manifest considerable inter-individual variation
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Serum pro-hepcidin concentrations and their responses to oral iron supplementation in healthy subjects manifest considerable inter-individual variation

  • Susanna Luukkonen und Kari Punnonen
Veröffentlicht/Copyright: 7. November 2006
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Abstract

Hepcidin participates in the regulation of iron homeostasis and its precursor pro-hepcidin can be measured in serum. We evaluated pro-hepcidin serum concentrations in healthy subjects and the possible effects of iron supplementation on the results. The results suggest extensive physiological variation in serum pro-hepcidin concentrations between healthy subjects with no symptoms or signs of anaemia, infections, inflammations, chronic disease or other interpretative factors. Before pro-hepcidin measurements can be used in clinical practise, further investigations are required to identify the physiological factors affecting normal serum pro-hepcidin variations in healthy subjects. The responses of serum pro-hepcidin to a 100-mg oral dose of iron also showed considerable inter-individual variation. In male subjects, no systematic changes in serum pro-hepcidin concentrations were found and the increase in serum iron was fairly modest. In nine out of the ten female subjects who had rather low amounts of storage iron, iron supplementation was followed by an increase in both serum iron and serum pro-hepcidin concentrations. There were considerable inter-individual differences in the timing and magnitude of the response. We also evaluated the conceivable influences of sample storage and freeze-thaw cycles on the results of serum pro-hepcidin ELISA. We did not observe any changes in the results after serum samples were frozen and thawed up to four times and/or stored at room temperature for up to 6h.

Clin Chem Lab Med 2006;44:1361–2.


Corresponding author: Susanna Luukkonen, MD, Laboratory Centre, Kuopio University Hospital, PL 1777, 70211 Kuopio, Finland Fax: +358-17-173200

References

1. Krause A, Neitz S, Mägert HJ, Schulz A, Forssmann WG, Schulz-Knappe P, et al. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. FEBS Lett 2000; 480:147–50.10.1016/S0014-5793(00)01920-7Suche in Google Scholar

2. Park CH, Valore EV, Waring AJ, Ganz T. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 2001; 276:7806–10.10.1074/jbc.M008922200Suche in Google Scholar PubMed

3. Ganz T. Hepcidin – a regulator of intestinal iron absorption and iron recycling by macrophages. Best Pract Res Clin Haematol 2005; 18:171–82.10.1016/j.beha.2004.08.020Suche in Google Scholar PubMed

4. Nemeth E, Valore EV, Territo M, Schiller G, Lichtenstein A, Ganz T. Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 2003; 101:2461–3.10.1182/blood-2002-10-3235Suche in Google Scholar PubMed

5. Dallalio G, Fleury T, Means Robert T Jr. Serum hepcidin in clinical specimens. Br J Haematol 2003; 122:996–1000.10.1046/j.1365-2141.2003.04516.xSuche in Google Scholar PubMed

6. Lehmann P, Niederau C, Bartel J, Klima H. Hepcidin a new marker in diagnosis of disorders of iron metabolism. Clin Chem 2004; 50(Suppl 6):A179.Suche in Google Scholar

7. Kulaksiz H, Gehrke SG, Janetzko A, Rost D, Bruckner T, Kallinowski B, et al. Pro-hepcidin: expression and cell-specific localization in the liver and kidney and its regulation in hereditary hemochromatosis, chronic renal insuffi-ciency and renal anemia. Gut 2004; 53:735–43.10.1136/gut.2003.022863Suche in Google Scholar PubMed PubMed Central

Received: 2006-7-14
Accepted: 2006-8-1
Published Online: 2006-11-7
Published in Print: 2006-11-1

©2006 by Walter de Gruyter Berlin New York

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