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Research Article

JCDR. 2021; 12(3): 1996-1998


Osama Nady Mohamed Abd El-Azeem; Ahmed Mohamed saad El-Deen Salama; Fatma El-Zahraa Sayed Bukhary; Asmaa Kasem Ahmed; Emad Allam abd El-Naem.


1 Hepcidin
1.1 Structure
In 2001, the hepcidin was identified and termed a peptide with anti-microbial effects (1). It consists of 84 amino acids and is known as preprohepcidin. The peptide is subsequently split together to generate a 60-amino-acid protein called prohepcidin and then processed to make a 25-amino-acid protein called hepcidin. Prohepcidine's last conversion to hepcidin is catalyzed by furin (2). The 25 amino acid peptides are the main form of human urine, despite the shorter peptides of 20 and 22 amino acids (3).
1.2 Synthesis
Systemic hepcidin can largely be found in the liver and can also be found in the renal tubules, the heart, the retina, fat, lungs and brains, stomach and pancreas. In unique biological liquors such as the bile, the ascetic, the pleural fluid and the cerebral fluid, hepcidin was also found (3). The bioactive type is hepcidin-25, a 25 amino acid peptide with a molecular weight of 2.8 kD. Hepcidin-20, -22, and -24 are hepcidin isoforms with no biological relevance (4). The production of hepatic hepcidin is boosted by high availability of iron and inflammation of the body. It is blocked by low flowing iron, erythropoiesis and hypoxia (5).
1.3 Kinetics
Hepcidin-25 either circulates freely or is bound to a minimum of α 2-macroglobulin, and albumin. The amount of hepcidin bound to protein is uncertain and the free circulating fracture varies between 11 to 98% (6). Protein-connected hepcidin may be biologically more active than hepcidin unbound (7). However, the fact that hepcidin clearance bound by protein is reduced, hence leading to an improved half-life and activity can be elucidated. Hepcidin is removed from its action and urine excretion sites by cellular breakdown. In healthy persons, hepcidin fractional excretion is low (not beyond 3 to 5 percent) (8), implied that hepcidin under normal conditions is either reabsorbed nearly fully in the renal tubule and depleted in the renal tubule (due to its protein-bound character) (9).

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