Human ProHAMP(Hepcidin prohormone) ELISA Kit

Hepcidin is an antimicrobial peptide produced by the liver that regulates iron metabolism in the body. It is encoded by the HAMP gene on chromosome 19, which is 2637 base pairs long and has two introns and three exons. The precursor form of Hepcidin is an 84-amino-acid peptide that undergoes post-translational changes to eventually create the physiologically active Hepcidin-25, which is composed of 25 amino acids. Hepcidin-25 has a positively charged N-terminal section and a C-terminal with four disulfide bridges in the cysteine residues, giving it a distinct amphiphilicity. Hepcidin's biological function is strongly tied to its structure and has a direct impact on iron homeostasis in the body. Iron, an essential trace element, plays a role in a variety of important biological activities, including oxygen transport, mitochondrial respiration, DNA synthesis, and other enzymatic reactions. Iron's redox characteristics serve an important function in cells, but they can also be damaging. Excess iron can cause the Fenton reaction to generate reactive oxygen species (ROS), such as extremely reactive hydroxyl radicals, which can damage DNA, proteins, and lipids, resulting in oxidative stress. Thus, maintaining iron balance is critical for regular physiological activities.

Hepcidin production and release are mostly controlled by the liver and are influenced by a number of other factors. The precursor peptide generated from the HAMP gene first undergoes post-translational changes in the Golgi apparatus before being transformed into the active form Hepcidin-25 by furin protease. Hepcidin-25 is then released into the bloodstream, where it exerts biological activity. Internal and external signals such as iron storage, hypoxia, inflammatory reactions, and erythropoiesis all influence Hepcidin production. Elevated iron levels in the body stimulate Hepcidin expression through the BMP-SMAD pathway, whereas iron deficiency and erythropoiesis expansion decrease Hepcidin production. Inflammation can also enhance Hepcidin expression via the IL-6/STAT3 signaling pathway, allowing the body to decrease iron release during infection or inflammation, hence decreasing pathogen proliferation. Hepcidin works primarily by binding to ferroportin, an iron transport protein on the cell membrane, and preventing the release of iron. The body's sole protein that exports iron is called ferroportin, which is found on the plasma membrane of macrophages and the basolateral side of intestinal epithelial cells. Hepcidin-25 reduces the amount of iron released into the bloodstream by binding to ferroportin and causing it to internalize and degrade. The body's ability to control its iron levels depends on this process. Enhanced ferroportin breakdown caused by elevated Hepcidin expression lowers systemic iron levels when iron levels are high or during inflammation. On the other hand, decreased Hepcidin expression supports iron mobilization and absorption during erythropoiesis expansion or iron deficit, preserving the regular iron supply.

Figure 1. Hepcidin regulates iron absorption and secretion (Source: Kowdley KV, et al., 2021)

Abnormal alterations in Hepcidin levels can have a major impact on iron metabolism. Elevated Hepcidin levels can cause iron deficiency anemia as well as inflammatory anemia. In such circumstances, iron is trapped in macrophages and intestinal epithelial cells, lowering plasma iron levels and causing anemic symptoms. These problems are frequently linked to chronic illnesses, inflammation, or infections. Low Hepcidin levels, on the other hand, can lead to iron overload, as seen in hereditary hemochromatosis and iron excess anemia. These disorders cause excessive iron accumulation in the body, which can lead to organ damage such as liver cirrhosis, cardiovascular disease, and endocrine dysfunction. Patients with iron overload frequently present with several problems, including liver damage, diabetes, and cardiovascular disease. In conclusion, Hepcidin, as a key iron-regulating factor, is critical in maintaining iron homeostasis by regulating the expression of iron transport proteins, effectively controlling iron distribution and release in the body, and preventing health problems caused by iron excess or deficiency. Understanding Hepcidin's biological activity and role in iron metabolism is critical for investigating and treating iron-related illnesses.

Prohepcidin ELISA Kit
Human Prohepcidin ELISA Kit
Hepcidin Prohormone ELISA Kit
ProHAMP ELISA Kit