Glycomic and sialoproteomic data of gastric carcinoma cells overexpressing ST3GAL4

Abstract

Gastric carcinoma MKN45 cells stably transfected with the full-length ST3GAL4 gene were characterised by glycomic and sialoproteomic analysis. Complementary strategies were applied to assess the glycomic alterations induced by ST3GAL4 overexpression. The N- and O-glycome data were generated in two parallel structural analyzes, based on PGC-ESI-MS/MS. Data on glycan structure identification and relative abundance in ST3GAL4 overexpressing cells and respective mock control are presented. The sialoproteomic analysis based on titanium-dioxide enrichment of sialopeptides with subsequent LC-MS/MS identification was performed. This analysis identified 47 proteins with significantly increased sialylation. The data in this article is associated with the research article published in Biochim Biophys Acta “Glycomic analysis of gastric carcinoma cells discloses glycans as modulators of RON receptor tyrosine kinase activation in cancer” [1].

Analysis of the Effect of Increased α2,3-Sialylation on RTK Activation in MKN45 Gastric Cancer Spheroids Treated with Crizotinib

“…Our results showed that the ST3GAL4 cell model displays a significant increase of α2,3-sialylation concomitant to a decrease of α2,6-sialylation. These results are in agreement with glycomic data previously reported [12,34]. In addition, a significant decrease in fucosylation, presumably outer arm fucosylation, was found as detected by Aleuria aurantia lectin (AAL).…”

“…Previous work disclosed that MET and RON downstream signaling is more activated upon overexpression of ST3GAL4 [11,12]. The expression of the SLeX epitope was detected by antibody-based assays, however, a detailed glycomic analysis by MS made clear that the most striking alteration in ST3GAL4 model was the general increase of α2,3-sialylation [34]. Increased sialylation on RTKs have been shown to play a role in tumor progression [11,41].…”

O‐glycan truncation enhances cancer‐related functions of CD44 in gastric cancer

“…The upregulation of ST3GAL4 in MKN45 leads to an increase in a2,3 sialylation and a decrease in a2,6 sialylation on N-glycans and significantly decreases the amount of bisected structures [45,50]. On O-glycans, ST3GAL4 leads to the earlier termination due to the increase in one specific structure: the di-sialylated core 2 structure [45,50]. Both the ST6GALNAC1 overexpression and the COSMC deletion induce alteration on O-glycans and lead to an upregulation of STn by two differential mechanisms [38,41].…”

“…1C,D) [30]. The M3 and ST3 models have previously been characterized by O-glycomic analysis and thus allowed us to estimate the induced alterations [45,50]. In this regard, the major O-glycans of M3 with the composition Hex-NAc 5 Hex 5 Neu5Ac 2 and HexNAc 4 Hex 4 Neu5Ac 2 , with the average masses of 2427.2 and 2061.9 Da, respectively, were altered in the ST3 model to HexNAc 2 Hex 2 Neu5Ac 2 , with an average mass of 1331.2 Da.…”

Targeting Aberrant Sialylation to Treat Cancer

“…Therapeutically, ST6GAL1 can be used to predict response to EGFR/HER2 inhibitors in ovarian cancer cells [34]. Similarly, ST3GAL4 is also upregulated in cancer, and is associated with poor prognosis; metastasis and the synthesis of Sialyl Lewix X (sLe X ) in gastric carcinoma [18,35]. ST3GAL6 is also linked to the synthesis of sLe X and the generation of E-selectin ligands [36,37].…”