Lactoferrin Structure Function and Genetics

Lactoferrin is an iron-binding glycoprotein that belongs to the transferrin family. It consists of two globular domains, called N-lobe and C-lobe. Both lobes have the similar polypeptide-folding pattern and one metal-binding site. Its structure is conserved among species. As well as other members of transferrin family, lactoferrin exerts their biological functions by chelating free irons in body fluids in mammals. Lactoferrin acts as bacteriostatic agent, based on their ability to deprive iron essential for bacteria growth. Besides, its iron-chelating activity, lactoferrin positively or negatively regulates host immune response by controlling maturation, migration, cytokine secretion of innate and adaptive immune cells. Lactoferrin is detected in many body fluids, and contributes host defense through the bactericidal and immuno-modulating activities. The difference of the lactoferrin expression among the different species and tissue could be explained by the diversity of lactoferrin gene promoter region.