Background: Fucosylated glycotopes of milk immunoglobulin G (IgG) are ligands in reactions of biological recognition protecting newborns against infection and ensuring proper development. Materials and methods: Relative amounts of IgG fucosyl-glycovariants in milk of mothers giving birth to term and premature newborns (term and preterm milk groups) were analysed by lectin-IgG-ELISA using a1,2-, a1,3-, and a1,6-fucose specific biotinylated Ulex europaeus (UEA), Tetragonolobus purpureus (LTA), and Lens culinaris (LCA) lectins, respectively. Results: The term and preterm milk IgG glycovariants were highly reactive with UEA, LTA, and LCA, whereas maternal plasma IgG poorly or at all. During milk maturation the IgG of very preterm and preterm milk compared to term milk differed by lower relative amounts of UEA-, higher of LTA-, and nearly stable expression of LCA-reactive glycotopes. Moreover, lower a1,2and higher [ 5 8 _ T D $ D I F F ] a1,3relative amounts of lectin-dependent milk IgG-fucosylated glycovariants were found to be associated with an infectious disease of lactating mothers. Conclusion:The highly fucosylated glycovariants of human IgG given with mothers' milk to immunologically immature newborn seem to be bifunctional molecules with potential therapeutic properties. The analysis of fucosylation status of milk IgG by simple lectin-IgG-ELISA may be helpful to control the immunological quality of milk for milk banking.

Background: Because terminal sugars of a-1-acid glycoprotein (AGP) are reported to be involved in antiinflammatory and immunomodulatory processes, their expressions might have an influence on the proper function of immune system of newborns. Here, relative amounts of sialylated and fucosylated glycotopes on human milk AGP over normal lactation were investigated. Materials and Methods: AGP concentration and relative amounts of its sialylated and fucosylated glycovariants were analyzed in early colostrum, colostrum, and transitional and mature milk samples of 127 healthy mothers by lectin-AGP enzyme-linked immunosorbent assay using a2,3-and a2,6-sialic acid and a1,2-, a1,3-, and a1,6-fucose specific biotinylated Maackia amurensis, Sambucus nigra, Ulex europaeus, Tetragonolobus purpureus, and Lens culinaris lectins, respectively. Results: AGP concentration in human milk was about 30 times lower than in plasma of lactating mothers and decreased gradually over lactation. Milk AGP showed significantly higher expression of sialylated and fucosylated glycotopes in comparison with those of plasma AGP. Milk AGP glycovariants containing a2,6-sialylated and a1,6-and a1,2-fucosylated glycotopes showed the highest relative amounts in early colostrums. With progression of lactation, the expressions of glycotopes a1,2-fucosylated decreased starting from Day 4 and those of a2,6-sialylated and a1,6-fucosylated from Day 8 of lactation, whereas the level of a2,3-sialyl-glycotope was almost constant over 45 days of lactation. In contrast, the expression of a1,3-linked fucose on AGP was low in colostrums and significantly higher in transitional and mature milk. Conclusions: The relative amounts of sialylated and fucosylated glycovariants of human hindmilk AGP significantly varied between Days 2 and 45 of normal lactation.

No abstract

Occurrence and relative amount of delivery-associated FN-fibrin complexes in both puerperal and cord plasmas might be bound with the physiological adaptive mechanisms reducing the risk of hemorrhage and intensive remodeling and repair processes after delivery.

Glycoproteins of human milk are multifunctional molecules, and their fucosylated variants are potentially active molecules in immunological events ensuring breastfed infants optimal development and protection against infection diseases. The expression of fucosylated glycotopes may correspond to milk maturation stages. The relative amounts of fucosylated glycotopes of human skim milk glycoproteins over the course of lactation from the 2nd day to the 47th day were analyzed in colostrums, transitional and mature milk samples of 43 healthy mothers by lectin-blotting using α1-2-, α1-6-, and α1-3-fucose specific biotinylated Ulex europaeus (UEA), Lens culinaris (LCA), and Lotus tetragonolobus (LTA) lectins, respectively. The reactivities of UEA and LCA with the milk glycoproteins showed the highest expression of α1-2- and α1-6-fucosylated glycotopes on colostrum glycoproteins. The level of UEA-reactive glycoproteins from the beginning of lactation to the 14th day was high and relatively stable in contrast to LCA-reactive glycoproteins, the level of which significantly decreased from 2–3 to 7–8 days then remained almost unchanged until the 12th–14th days. Next, during the progression of lactation the reactivities with both lectins declined significantly. Eighty percent of α1-2- and/or α1-6-fucosylated glycoproteins showed a high negative correlation with milk maturation. In contrast, most of the analyzed milk glycoproteins were not recognized or weakly recognized by LTA and remained at a low unchanged level over lactation. Only a 30-kDa milk glycoprotein was evidently LTA-reactive, showing a negative correlation with milk maturation. The gradual decline of high expression of α1-2- and α1-6-, but not α1-3-, fucoses on human milk glycoproteins of healthy mothers over lactation was associated with milk maturation.