Altered Glycosylation in Prostate Cancer

Identification of IgM as a contaminant in lectin-FLISA assays for HCC detection

“…Glycosylation changes have been observed in many cancers, including but not limited to liver[13–16], pancreas[17–20], lung [21, 22], breast [23], ovarian[24], colon[25] and prostate cancer[26, 27]. In many, proteins that contain these glycan changes have been identified.…”

Glycosylation and Cancer: Moving Glycomics to the Forefront

“…The implications that tumor cells modulate miRNA networks to alter glycosylation profiles associated with cancer development and progression could be a transformative concept that will need to be assessed in each type of cancer for similarities and differences in miRNA participants. Another emerging area that merges all of the "omics" discussed is that of glycosylation in cancer exosomes/microvesicles (Drake et al, 2015;Drake & Kislinger, 2014;Liang et al, 2014). The unique lipid, glycan, protein, and miRNA components of exosomes reflect their cancer type origins and are attractive targets for development of biomarkers, especially miRNAs.…”

“…Glycosidases with enzymatic specificity for anomeric configuration and sugar composition, or lectins with this level of specificity, have been traditionally combined with MALDI analysis to provide additional structural information. New high-resolution FTICR-MALDI instruments also offer some analytical improvements, and progress in this area has been recently assessed (Leymarie et al, 2013) and summarized in this volume (Drake et al, 2015;Holst et al, 2015). As highlighted for a multilaboratory analysis of prostate-specific antigen (PSA) (Leymarie et al, 2013), there has been significant development of analytical methods and tools to determine the range of glycan heterogeneity at the single site of glycosylation of PSA.…”

“…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.…”

Glycans and glycoproteins as specific biomarkers for cancer

“…Other glycosylated protein markers include prostate-specific antigen (PSA), which is present in elevated amounts in seminal fluids and plasma, for screening and monitoring prostate cancer patients [43,44]. Carcinoembryonic antigen (CEA), which has been found to change in colorectal, bladder, breast, pancreatic and lung cancer, is highly N-glycosylated [45–47].…”