dc.contributor.author | Wilson, Nicole L. | |
dc.contributor.author | Robinson, Leanne J. | |
dc.contributor.author | Donnet, Anne | |
dc.contributor.author | Bovetto, Lionel | |
dc.contributor.author | Packer, Nicolle H. | |
dc.contributor.author | Karlsson, Niclas G. | |
dc.date.accessioned | 2018-09-20T16:28:32Z | |
dc.date.available | 2018-09-20T16:28:32Z | |
dc.date.issued | 2008-09-05 | |
dc.identifier.citation | Wilson, Nicole L. Robinson, Leanne J.; Donnet, Anne; Bovetto, Lionel; Packer, Nicolle H.; Karlsson, Niclas G. (2008). Glycoproteomics of milk: differences in sugar epitopes on human and bovine milk fat globule membranes. Journal of Proteome Research 7 (9), 3687-3696 | |
dc.identifier.issn | 1535-3893,1535-3907 | |
dc.identifier.uri | http://hdl.handle.net/10379/14442 | |
dc.description.abstract | Oligosaccharides from human and bovine milk fat globule membranes were analyzed by LC-MS and LC-MS/MS. Global release of N-linked and O-linked oligosaccharides showed both to be highly sialylated, with bovine peak-lactating milk O-linked oligosaccharides presenting as mono- and disialylated core 1 oligosaccharides (Gal beta 1-3GalNAcol), while human milk had core type 2 oligosaccharides (Gal beta 1-3(GlcNAc beta 1-6) GalNAcol) with sialylation on the C-3 branch. The C-6 branch of these structures was extended with branched and unbranched N-acetyllactosamine units terminating in blood group H and Lewis type epitopes. These epitopes were also presented on the reducing terminus of the human, but not the bovine, N-linked oligosaccharides. The O-linked structures were found to be attached to the high molecular mass mucins isolated by agarose-polyacrylamide composite gel electrophoresis, where MUC1 and MUC4 were present. Analysis of bovine colostrum showed that O-linked core 2 oligosaccharides are present at the early stage (3 days after birth) but are down-regulated as lactation develops. This data indicates that human milk may provide different innate immune protection against pathogens compared to bovine milk, as evidenced by the presence of Lewis b epitope, a target for the Helicobacter pylori bacteria, on human, but not bovine, milk fat globule membrane mucins. In addition, non-mucin-type O-linked fucosylated oligosaccharides were found (NeuAc-Gal-GlcNAc1-3Fuc-ol in bovine milk and Gal-GlcNAc1-3Fuc-ol in human milk). The O-linked fucose structure in human milk is the first to our knowledge to be found on high molecular mass mucin-type molecules. | |
dc.publisher | American Chemical Society (ACS) | |
dc.relation.ispartof | Journal of Proteome Research | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Ireland | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/ie/ | |
dc.subject | milk | |
dc.subject | muc1 | |
dc.subject | muc4 | |
dc.subject | mucin | |
dc.subject | egf | |
dc.subject | bacterial adhesion | |
dc.subject | monoclonal-antibodies | |
dc.subject | sialomucin complex | |
dc.subject | mammary-gland | |
dc.subject | oligosaccharides | |
dc.subject | mucin | |
dc.subject | purification | |
dc.subject | inhibition | |
dc.subject | pathways | |
dc.subject | infants | |
dc.subject | cancer | |
dc.title | Glycoproteomics of milk: differences in sugar epitopes on human and bovine milk fat globule membranes | |
dc.type | Article | |
dc.identifier.doi | 10.1021/pr700793k | |
dc.local.publishedsource | http://pubs.acs.org/doi/pdf/10.1021/pr700793k | |
nui.item.downloads | 0 | |