Known for some time (discovered by Sorensen and Sorensen in cow's milk in 1939), it has recently been re-evaluated for its antioxidant, immunomodulatory and anti-infective properties.
Typical of milk, as the name suggests, lactoferrin is also present in various mucous secretions, such as tears and saliva.
More abundant in colostrum than transition and maintenance milk, lactoferrin is also typical of neutrophil granulocytes, immune cells with defense functions against bacterial and fungal infections.
Its natural biological function also significantly affects its clinical potential.
According to further pharmacokinetic works, however still to be confirmed, lactoferrin could be absorbed as it is by enterocytes, thus extending its functions also at the systemic level.
, Proteus Mirabilis, Staphylococcus aureus, Candida albicans and others.This activity seems to be linked in part to the ability of lactoferrin to inhibit bacterial adhesion to the intestinal mucosa, and in part to the ability to firmly bind iron, making it unavailable to the pathogenic microorganism.
This would prevent the growth and proliferation of the microorganism.
Lactoferrin and antiviral activity
The antiviral activity of Lactoferrin - effective against viruses such as HIV, Herpes Simplex and Cytomegalovirus - seems to be attributable to its ability to inhibit the fusion between virus and cell by binding glycosaminoglycans.
Lactoferrin and immunomodulatory activity
According to some authors, lactoferrin could promote the differentiation and growth of T lymphocytes and at the same time modulate the expression of inflammatory cytokines.
This activity would be valuable in modulating the immune defenses both in the course of infectious and autoimmune pathologies.
Lactoferrin and antioxidant activity
The ability of lactoferrin to bind the ferric ion (Fe3 +) is twice higher than transferrin, the main plasma protein responsible for transporting iron in the bloodstream (both are part of the same family of proteins - called transferrins - capable of binding and transferring ions Fe3 +). Each lactoferrin molecule can bind two ferric ions to itself and based on this saturation it can exist in three distinct forms: apolactoferrin (iron-free), monoferrin lactoferrin (linked to a single ferric ion) and ololactoferrin (which binds two ions to itself ferrici).
This ability could be valuable in the redox balance, preventing the iron from reacting in the dreaded Fenton reaction, forming highly reactive oxidative species.
In most cases, lactoferrin is associated with probiotics, microorganisms with a protective function, or with prebiotics, nourishment for the intestinal flora.
, very rare, the use of lactoferrin, according to the appropriate indications, is generally safe and well tolerated.
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and in the subsequent period of breastfeeding, given the absence of long-term studies on the safety profile of this molecule.
