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. 2015 Jun 25;6(6):e1796. doi: 10.1038/cddis.2015.174

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Copyright © 2015 Macmillan Publishers Limited

Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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Characterization of glycation of VN by MGO. (a) Glycation of VN. Multimeric VN (10 μg/ml) and monomeric VN (10 μg/ml) were treated with MGO (500 μmol/l) at 37 °C for 72 h and samples were separated by SDS-PAGE under reducing and non-reducing conditions. Mult-VN, multimeric VN; Mono-VN, monomeric VN; MGO, methylglyoxal. (b) Mass spectra from the glycated VN reveals O-glycosylation on T55 in the tryptic peptide TAECK. (c) Schematic domain organization of human VN. Glycosylation sites linked to one O-glycosylation onT55 and three N-glycosylation sites at N86, N169 and N242 are marked by hexagons