Description
Hepcidin-25 is a cysteine-rich peptide that is produced in the liver from an 84-amino acid precursor, pre-hepcidin.
So far, four isoforms have been characterised, which are distinguished by amino-terminal truncations: hepcidin-20, -22, -24 and -25. Hepcidin-20 and -25 are the two main forms consisting of 20 and 25 amino acids, respectively. Mass spectrometric analysis allows the differentation of these two isoforms and thus the selective determination of hepcidin-25. The natively folded hepcidin-25 contains eight cysteines linked by intramolecular disulfide bridges and regulates, among other things, the absorption of iron into the body.
Binding of hepcidin-25 to ferroportin, the iron export channel, eventually leads to lyosomal degradation of ferroportin. This inhibitory binding prevents the absorption of iron into the bloodstream. Hepcidin-25 can be used as a predictor of iron absorption. Hepcidin-25 enables the differentation of iron deficiency anemia (IDA) from anemia in chronic diseases (ACD) and ACD/IDA. It also predicts the response to oral iron therapy and thus provides valuable information for the treatment of patients.
