Lactoferrin is a multifunctional mammalian immunity protein that limits microbial growth through sequestration of nutrient iron. Additionally, lactoferrin possesses cationic protein domains that directly bind and inhibit diverse microbes. The implications for these dual functions on lactoferrin evolution and genetic conflicts with microbes remain unclear. Here we show that lactoferrin has been ...

Nonresolving inflammatory processes affect all stages of carcinogenesis. Lactoferrin, a member of the transferrin family, is involved in the innate immune response and anti-inflammatory, anti-microbial, and anti-tumor activities. We previously found that lactoferrin is significantly down-regulated in specimens of nasopharyngeal carcinoma (NPC) and negatively associated with tumor progression, m...

OBJECTIVE To describe mechanisms of action of human lactoferrin to protect gastrointestinal morbidities. DATA SOURCES Nonsystematic literature review using the following databases: SciELO, Lilacs and Medline from 1990 to 2011. The key-words used were lactoferrin, human milk/breastfeeding, gastrointestinal, and immunity, in Portuguese and English. DATA SYNTHESIS Lactoferrin is the second pre...

Lactoferrin was purported in consumer literature to enhance and support the immune system response through their antioxidant, antibacterial, and anticarcinogenic properties. To improve the effectiveness of lactoferrin, liposomes were used as a carrier in this study. The main purpose of this study was to compare three different methods to prepare the lactoferrin nanoliposomes based on the encaps...

Lactoferrin is a glycoprotein present in most human mucosal secretions, including human milk. Lactoferrin is bacteriostatic in low iron media and, in some settings, bactericidal. Lactoferrin impairs ability of Shigella flexneri serotype 5 strain M90T to invade HeLa cells. To determine the mechanism by which lactoferrin decreases invasiveness of Shigella organisms, its effect on the major virule...

The binding of lomefloxacin to bovine lactoferrin (BLf) in a dilute aqueous solution was studied using fluorescence spectra. The binding constant (K) and the number of binding sites (n) were obtained by a fluorescence quenching method. The binding distance (r) and energy-transfer efficiency (E) between lomefloxacin and bovine lactoferrin were also obtained according to the mechanism of Foörster...

Using commercially available reagents we developed an enzyme-linked immunosorbent assay to measure lactoferrin in normal human tears. Tears obtained from 38 normal human subjects contained a mean lactoferrin content of 2.2 mg/ml (g/l). No differences in the mean level of lactoferrin were found when tears were collected by either Schirmer tear strips or by glass capillaries after short tear gas ...

This review discusses the biological properties of the glycoprotein lactoferrin. Lactoferrin has been identified in secretions from exocrine glands and in specific granules of neutrophils. After degranulation, neutrophils become the main source of lactoferrin in blood plasma. Lactoferrin possesses various biological functions, including roles in iron metabolism, cell proliferation and different...

The possibility that the presence of lactoferrin in aspirates of odontogenic cyst fluid might be a useful preoperative diagnostic marker for odontogenic keratocyst was investigated. Using qualitative and quantitative immunodiffusion methods fluid from 29 of 29 dental (radicular) cysts, 12 of 14 dentigerous cysts and 27 of 31 keratocysts were found to contain lactoferrin. Although some of the hi...

Previous studies have shown that Gardnerella vaginalis can utilize iron-loaded human lactoferrin as a sole source of iron. In this study, G. vaginalis cells were shown to bind digoxigenin (DIG)-labeled human lactoferrin in a dot blot assay. Using the DIG-labeled human lactoferrin, a 120-kDa human lactoferrin-binding protein was detected by Western blot analysis of G. vaginalis proteins. The lac...