Immunomodulatory effects of lactoferrin

Abstract

Lactoferrin (Lf) is an iron-binding glycoprotein of the transferrin family, which is expressed in most biological fluids with particularly high levels in mammalian milk. Its multiple activities lie in its capacity to bind iron and to interact with the molecular and cellular components of hosts and pathogens. Lf can bind and sequester lipopolysaccharides, thus preventing pro-inflammatory pathway activation, sepsis and tissue damages. Lf is also considered a cell-secreted mediator that bridges the innate and adaptive immune responses. In the recent years much has been learned about the mechanisms by which Lf exerts its activities. This review summarizes the recent advances in understanding the mechanisms underlying the multifunctional roles of Lf, and provides a future perspective on its potential prophylactic and therapeutic applications.

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

“…Tests carried out on mandarins with bLfcin and Lf (17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31) showed a significant protection against Penicillium digitatum at a concentration close to the in vitro MIC value [115]. More recently Baruzzi et al demonstrated the interesting activity of bLfcin in controlling microbial spoilage in ready-to-eat leafy vegetables during cold storage [116].…”

Impact of Dental Plaque Biofilms in Periodontal Disease: Management and Future Therapy

“…Lactoferrin is an iron-binding glycoprotein that links to free iron in the saliva, causing bactericidal or bacteriostatic effects on various microorganisms requiring iron for their survival. Lactoferrin also provides fungicidal, antiviral, anti-inflammatory, and immunomodulatory functions [31][32][33]. The lactoperoxidase-thiocyanate system in saliva has been shown to be bactericidal on some strains of Lactobacillus and Streptococcus by preventing the accumulation of lysine and glutamic acid, both of which being essential for bacterial growth [34,35].…”

Injuries in Thai Boxing

“…Each lobe has one binding site for iron ions (Fe +2 or Fe +3 ), and one or more potential glycosylation sites, depending on the species from which LF is isolated. Depending on its form, the molecular weight of LF varies between 76 and 80 kD (Levay, Viljoen, 1995;Siqueiros-Cendón et al, 2014). The degree of iron saturation determines the spatial structure of LF, which occurs in two forms: apolactoferrin (apo-LF), with low iron saturation, and iron-rich hololactoferrin (holo-LF) (Baker, Baker, 2005).…”

“…Acting via two mechanisms of intracellular signal transduction, i.e. nuclear factor kappa B and MAP kinase, LF modulates differentiation, maturation, activation, migration, proliferation and function of immune cells, T and B cells, neutrophils, monocytes/macrophages and dendritic cells belonging to the antigen-presenting cells (APC) (Gahr, Speer, Damerau, Sawatzki, 1991;Krzyżowska, Świątek, Fijałkowska, Niemiałtowski, Schollenberger, 2009;Siqueiros-Cendón et al, 2014) (Figure 3).…”

“…They also participate in adaptive immune system by stimulating specific T cells after antigen presentation. In vitro studies have shown that both human and bovine macrophages contain surface receptors for LF (Birgens, Hansen, Karle, Kristensen, 1983;Roseanu, Chelu, Trif, Motaş, Brock, 2000;Siqueiros-Cendón et al, 2014). LF is also involved in the suppression of proinflammatory cytokines and induction of interferon α/β (IFN/β), and affects the ability of macrophages to present antigens to CD4 + T cells in the adaptive resistance (Latorre, Puddu, Valenti, Gessani, 2010;Siqueiros-Cendón et al, 2014).…”