A quantitative N-glycoproteomics study of cell-surface N-glycoprotein markers of MCF-7/ADR cancer stem cells

N-Glycoproteomics Study of Putative N-Glycoprotein Biomarkers of Drug Resistance in MCF-7/ADR Cells

“…and CSC N-glycosylation markers (centrosome-associated protein 350 CE350, zinc finger protein GLI1, CD63 antigen and CD13 etc.) were reported in our previous studies (Wang et al 2020b;Xu et al 2020).…”

“…5). This intact N-glycopeptide SLSNSTAR_N2H5F0S0 (P50454, SERPH_ HUMAN, N120) was also quantified in our previous studies (Wang et al 2019(Wang et al , 2020b. For lysosome-associated membrane glycoprotein 1 (P11279, LAMP1_HUMAN), intact N-glycopeptides GHTLTLNFTR with N2H6F0S0 and N2H7F0S0 on N-glycosite N103 were quantified with fold changes of 1.79 ± 0.38 and 0.89 (only quantified once in spectrum 20,345 of TR2), respectively.…”

“…Hence, it is still urgent to figure out the mechanisms of drug resistance. In this regard, intact N-glycoproteins about the development of drug resistance, either identified or quantified in current and previous studies (Wang et al 2019(Wang et al , 2020bXu et al 2020;Xue et al 2020), were discussed.…”

A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry–Based Glycoproteomics

“…HILIC enrichments have been used to enrich glycopeptides from a wide range of biological matrices, including human biofluids ( e.g. , plasma, serum, and milk) ( 209 , 210 , 211 , 212 , 213 , 214 ), cancer systems ( 215 , 216 , 217 , 218 , 219 , 220 , 221 ), other human model systems ( 222 , 223 ), murine tissues ( 178 , 224 , 225 , 226 , 227 ), pathogens ( 228 , 229 , 230 , 231 ), and plants ( 232 ). HILIC has been used both as stand-alone and in combination with IMAC and MOAC to enrich phospho- and glycopeptides, too, as mentioned above.…”

Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation

“…Novel applications include the association of altered glycopeptide glycosylation profiles with pancreatic cancer ( 117 ), glycoproteomic profiling in triple-negative breast carcinomas through analysis of deglycosylated peptides ( 118 ), quantitative comparisons of sialic-acid-containing glycopeptides in human embryotic and neural stem cells ( 119 ), and employing deglycosylated peptides to determine changes in site occupancy rates between normal liver and hepatocellular carcinoma (HCC) liver tissues ( 120 ). Further development of this strategy has been seen in the employment of diethyl labeling of glycopeptides ( 121 , 122 , 123 ), which reduces retention time differences and quantitation errors by replacing and incorporating heavy carbon in place of deuterium.…”