J Appl Biomed 15:196-203, 2017 | DOI: 10.1016/j.jab.2017.02.001
Alpha 2,3- and alpha 2,6-sialylation of human skim milk glycoproteins during milk maturation
- a Department of Chemistry and Immunochemistry, Wroclaw Medical University, Wroc³aw, Poland
- b Independent Public Clinical Hospital No 1, Wroc³aw, Poland
Human milk is a source of glycoconjugates, sialylated forms of which enrich the newborn immature immune system and are crucial for their proper development and well-being. Here, we analyzed the expression of α2,3-/α2,6-sialylated glycotopes on skim milk glycoproteins over lactation. Milk samples were analyzed by lectin-blotting using α2,3- and α2,6- sialic acid specific Maackia amurensis (MAA) and Sambucus nigra (SNA) lectins and sialyl- and asialyl-T antigen specific Artocarpus integrifolia (Jacalin) and Arachis hypogaea (PNA) lectins. The reactivities of MAA, SNA, Jacalin and PNA with milk glycoproteins showed that they are heavily decorated with α2,3-/α2,6-linked sialic acid and sialyl-T antigen and to a lesser degree with asialyl-T antigen. Despite individual differences of particular glycoproteins, a sharp and significant decline of α2,6-sialylated glycotopes and sialyl-T antigens and a weaker but significant decrease of α2,3-sialylated glycotopes and asialyl-T antigens on milk glycoproteins during milk maturation was observed. The expression of α2,3-/α2,6-sialylated glycotopes, sialyl- and asialyl-T antigens corresponds to milk maturation but differs in relation to the analyzed glycoprotein. Sialylated milk glycoproteins are considered as a part of innate immunity provided to neonates. Further investigations are needed to understand if they may be useful in milk banking to control the biochemical quality of milk.
Keywords: Human milk glycoproteins; Alpha 2,3- and alpha 2,6-sialylated glycotopes; Lactation; Lectins; Sialic acid; T antigen
Received: August 19, 2016; Revised: January 31, 2017; Published: July 1, 2017 Show citation
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