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. 2014 May;75(5):675-9.
doi: 10.1038/pr.2014.24. Epub 2014 Feb 12.

Recent advances in human milk glycobiology

David S Newburg  1 , Gilman Grave  2
Affiliations

Recent advances in human milk glycobiology

David S Newburg et al. Pediatr Res. 2014 May.
No abstract available

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Figures

Figure 1
Figure 1
Sites of human milk glycan activity. The primary site for HMOS activity is the lumen of the gut, as the preponderance of HMOS are not digested or absorbed. However, those HMOS that are absorbed are excreted into the urine, and there they could inhibit uropathogenic organisms. The mechanisms whereby orally ingested HMOS affect sites distant from the gut are unknown, but can be speculated to be a direct affect of HMOS in the bloodstream, modulation of the global mucosal immune system through a primary affect on intestinal mucosal immune status, or mediated through secondary metabolites of HMOS fermentation in the gut that traverse the bloodstream.
Figure 2
Figure 2
Human milk oligosaccharides (HMOS). The human milk oligosaccharides contain lactose on the reducing end, and most contain a polylactosamine backbone. In contrast to bovine milk, human milk oligosaccharides are a major component, with the majority being fucosylated. The acidic oligosaccharides contain sialic acid.
Figure 3
Figure 3
Human milk glycoconjugates (HMG). Most of the major macromolecules of human milk are glycosylated, many heavily. The principal families of glycoconjugates in milk include the mucins, glycosaminoglycans, glycoproteins, glycopeptides, and glycolipids, with examples depicted in this figure. Sugar abbreviations: GalNAc, N-acetylgalactosamine; GlcNAc, N-acetylglucosamine; Gal, galactose; Glc, glucose; Man, mannose; Fuc, fucose; Xyl, xylose; sialic acid, N-acetylneuraminic acid (some N-glycolylneuraminic acid; GlcA, glucuronic acid; IdoA, iduronic acid.
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References

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    1. Newburg DS, Neubauer SH. Carbohydrates in Milks: Analysis, Quantities, and Significance. In: Jensen RG, editor. Handbook of Milk Composition. San Diego, California, USA: Academic Press; 1995. pp. 273–349.
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