Functional Impact of Tumor-Specific N-Linked Glycan Changes in Breast and Ovarian Cancers

Tissue glycomics distinguish tumour sites in women with advanced serous adenocarcinoma

“…This nonreducing end terminal group is rare on mammalian glycoproteins, and can be further modified with sialic acid, fucose and sulfate (Hirano et al ., ). In agreement with this finding, we have previously identified LacdiNAc‐type N ‐glycans in ovarian cancer cell lines but not on normal HOSE cell line membrane proteins (Anugraham et al ., ) and this glycan motif was also reported to be a tumour‐specific glycan in breast and ovarian cancer cell lines investigated in a separate study (Guo and Abbott, ). In this tissue‐based study, we identified three sialylated LacdiNAc‐type N ‐glycans ( m / z 1205.0 2− , m / z 1059.4 2− and m / z 1079.9 2− ) that were capable of distinguishing OC from PC, and these glycans, together with an additional nonsialylated LacdiNAc‐type N ‐glycan ( m / z 913.9 2− ), were all found to be associated with ovarian cancer‐derived tissues only.…”

Glycans and glycoproteins as specific biomarkers for cancer

“…Other types of glycans include glycosaminoglycans usually found attached to the proteins (proteoglycans) and also lipid chains as in glycolipids [77]. There is now a considerable body of work showing that glycans released from cancer cells differ from those in healthy cells [76,78–80,71,81]. Tumors have been found to overexpress certain types of glycoproteins and glycolipids [80,82].…”

“…There is now a considerable body of work showing that glycans released from cancer cells differ from those in healthy cells [76,78–80,71,81]. Tumors have been found to overexpress certain types of glycoproteins and glycolipids [80,82]. For example, there is an increase in the size and branching of N-glycans in tumors [76].…”

Glycosylation and Cancer: Moving Glycomics to the Forefront

“…In an attempt to provide the broadest scope possible for this current volume, leading investigators at the forefront of current research on the roles of N-linked glycans, O-linked glycans, and O-GlcNAc modifications in cancer have contributed detailed overview chapters of their respective subjects (Kudelka, Ju, Heimburg-Molinaro, & Cummings, 2015;Nagel & Ball, 2015;Taniguchi & Kizuka, 2015). The remaining chapter contributors were all asked to summarize the functions and research progress made for the roles of glycosylation in specific types of cancers, including pancreas (Tang, Hsueh, Kletter, Bern, & Haab, 2015), colon (Holst, Wuhrer, & Rombouts, 2015), ovarian and breast (Guo & Abbott, 2015), brain and lung (Lemjabbar-Alaoui, McKinney, Yang, Tran, & Phillips, 2015), liver (Mehta, Herrera, & Block, 2015), and prostate (Drake, Jones, Powers, & Nyalwidhe, 2015). The collective volume represents an excellent summary of what has been accomplished for each type of major O-linked and N-linked glycan species, glycolipids, and glycosaminoglycans, as well as what is known about specific glycans associated with each individual cancer type.…”