Hepcidin is a peptide that was discovered in 2000, it is synthesized
in the liver and it goes into circulation. There are three forms of
hepcidin, hepcidin-25, hepcidin-22 and hepcidin-20. The first
form is the most studied and its role is the most significant.
Hepcidin-25 is considered to be a major regulator of the
absorption of dietary iron as well as its release from cells. It
achieves its regulatory function by preventing the function
of ferroportin, the major cellular iron exporter. Ferroportin
is a protein whose function is to release iron from the cells on
which it is located (macrophages, hepatocytes and enterocytes).
Hepcidin-25 induces degradation of ferroportin, resulting
in an increase in intracellular iron stores. It also reduces the
absorption of iron from food and thus reduces the concentration
of circulating iron. During physical activity, the concentration
of hepcidin increases at an intensity of 65% VO2
max, and
maximum values are reached at 90-95% VO2
max. Not only
intensisty, but also the volume of physical activity influence its
concentration. Sudies showed that hepcidin expression during
physical activity is influenced by inflammation, iron status,
erythropoiesis and hypoxia. It is considered one of the causes of
anemia in athletes. There are potential methods for neutralizing
hepcidin (monoclonal antibodies and antagonists) and reducing
its expression (erythropoietin doping, wich is forbbiden in
sport, anti-IL-6 antibodies, STAT and BMP modulators). Given
its important role in iron metabolism, which is essential for the
transport of oxygen in the body, it can affect sports performance.
It is still the subject of many research.