The expression of fucose isoforms of amniotic and plasma alpha-1-acid glycoprotein derived from 2nd and 3rd trimester normal pregnancies

Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

“…That fact was probably linked with pregnancy, delivery, and postpartum hormonal imbalance, 32 which may lead to individual response and modulation of synthesis of Lewis x antigen. Although according to Froehlich et al 2 there is no common pattern for the alterations of particular milk glycoproteins during lactation, the sialylation and fucosylation changes are more or less similar to those of third-trimester amniotic AGP, 14,15 other milk glycoproteins, 7,8 and abundantly present HMOs. 4,30,31 It seems likely that the same set of glycosyltransferases is involved in elongation and branching of glycans of glycoconjugates and HMOs in lactating mammary glands.…”

“…Sialyl-and fucosyl-glycotope expression on a constant amount (100 ng) of AGP was determined by lectin-AGP ELISA according to a slightly modified procedure described earlier 14,15 using specific biotinylated lectins (Vector Laboratories, Inc., Burlingame, CA) with well-described binding preferences. 23 MAA and SNA are known to have binding preferences to sialic acid linked by anomeric glycosidic a2,3 and a2,6 linkages, respectively.…”

“…The glycans can be bi-, tri-, or tetra-antennary and are terminated by sialic acid and fucose in varying degrees. 9,13 Alteration of AGP glycosylation is tissue-specific and is reported to be associated with normal and pathological pregnancy, [14][15][16] as well as with inflammation, cancer, liver abnormalities, and cardiovascular diseases. 9 Fetal AGP has a different oligosaccharide pattern compared with that of an adult and carries three N-and three O-linked oligosaccharide chains and unusual lactosamine structural motifs.…”

“…Amniotic AGP elicits alterations in glycan part, particularly an increase in branching of N-glycans as well as in the degree of fucosylation and sialylation. [13][14][15] The glycans of AGP are reported to influence its biological activities and to modulate cell-to-cell interactions and cellular signaling. 9,17 During the inflammatory process the sialylated and fucosylated glycotopes of AGP are reported to be involved in anti-inflammatory and immunomodulatory reactions.…”

Terminal glycotope expression on milk fibronectin differs from plasma fibronectin and changes over lactation

“…Expression of sialyl-and fucosyl-glycotopes as well as T and Tn antigens on a constant amount (50 ng) of FN was determined by lectin-FN-ELISA according to a slightly modified procedure described earlier [16,18] using specific biotinylated lectins (Vector Laboratories, Inc., Burlingame, CA, USA) with well-described binding preferences described by Wu et al [19]. MAA (M. amurensis agglutinin) and SNA (S. nigra agglutinin) have the abilities to bind sialic acid linked by anomeric glycosidic α2,3 and α2,6 linkages Gal/GalNAc, respectively.…”