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. 2020 Apr 21;10:496. doi: 10.3389/fonc.2020.00496

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Copyright © 2020 Zhao, Jia, Li, Ma, Wu, Shen, Dang, Zhu, Li, Zhi, Lan, Xu, Hao, Chai, Li, Hu and Sun.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Large-scale profiling of intact glycopeptides in HCC tumors and paired paracancer tissues. (A) Profiling of N-linked glycans at individual glycosylation sites identified from all HCC tumor and paracancer samples. The peptide-spectrum-matches (PSMs) of each out of 4,741 intact glycopeptides, comprising of 221N-glycans (upper) and 894 glycosites (left), were exhibited in the heat map with different colors. The numbers of glycosites modified by each glycan and of glycans at each glycosite were summarized at the bottom and right parts of the figure, respectively. N: HexNAc; H: Hex; F: Fucose; S: Sialic acid. (B) The PSM percentages of different glycans based on glycan subtypes, antennary numbers, as well as the numbers of sialic acid and fucose modifications. (C) Top ten glycans detected from all HCC tumor and paracancer tissue samples based on the numbers of their modified glycosylation sites.