Hepcidin 25 LC-MS/MS

Hepcidin is a small cystein-rich peptide produced in the liver. It regulates the absorption
of iron in the body. Hepcidin was initially isolated as a circulating, antimicrobial
25 amino acid peptide in human urine and blood. Human hepcidin is synthesized
as prohepcidin, a 84 amino acid precursor, including a putative signal peptide of
24 amino acids. From human urine, two predominant forms, hepcidin-20 and hepcidin-25,
differing by amino-terminal truncation, were characterized as 20 and 25 amino
acid residues with 8 cysteines connected by intramolecular disulfide bonds. An
over-expression of hepcidin was shown to result in severe iron deficiency anemia
in transgenic mice, indicating that hepcidin plays a pivotal role in iron metabolism.
Recent studies have found abnormal hepcidin expression and disrupted hepcidin regulation
in hemochromatosis gene. A disturbed hepcidin regulation mechanism has
a direct effect on the iron metabolism in the organism. Decreased hepcidin expression,
e.g. due to a genetic defect, results in a direct iron overload, known as the iron
disease hemochromatosis. Based on these observations, it has been suggested that
hepcidin is a key component of iron homeostasis that acts as a negative regulator of
iron absorption in the small intestine and of iron release from macrophages.
Hepcidin can be used independently of accompanying diseases as an early predictive
marker for functional iron deficiency and/or anomalous iron utilization.