ST6GalNAc Inhibitor Development Service
Solutions of ST6GalNAc Inhibitor Development
N-Acetyl-galactosamine α-2,6-sialyltransferase (ST6GalNAc) family contains six ST6GalNAc proteins in mammals, namely ST6GalNAc I-VI. Sialyltransferases of the same family have some overlapping but not identical receptor substrate specificities. Among them, ST6GalNAc I, II, and IV catalyze the formation of α-2,6-bonds to GalNAc residues and O-glycosidic linkage to Ser/Thr; the remaining three mainly catalyze the addition of salivary acid residues to gangliosides. Based on the six ST6GalNAc proteins, we offer corresponding inhibitor development services to optimize efficacy.
Tab.1 Summary of ST6GalNAc family specificity. (Crespo, et al., 2013)
| Sialyltransferase | Preferred saccharide substrate | Glycan specificity |
| ST6GalNAc-I | GalNAcα1, O-Ser/Thr Galβ1,3GalNAcα1, O-Ser/Thr |
O-glycan |
| ST6GalNAc-II | Galβ1,3GalNAcα1, O-Ser/Thr | O-glycan |
| ST6GalNAc-III | Siaα2,3Galβ1,3GalNAc | O-glycan |
| ST6GalNAc-IV | Siaα2,3Galβ1,3GalNAc | O-glycan |
| ST6GalNAc-V | GM1b | Glycolipid |
| ST6GalNAc-VI | All α-series gangliosides | Glycolipid |
ST6GalNAc Inhibitor Development Service at CD BioGlyco
Sialylated antigen (STn) is rarely expressed in healthy tissues but is aberrantly expressed in multiple cancer cells. Overexpression of STn is caused by aberrant expression of ST6GalNAc, and serum STn levels are used as a marker of cancer invasive and metastatic potential. Thus, ST6GalNAc is well suited for the development of cancer inhibitors. We provide highly efficient and rapid ST6GalNAc inhibitor development services to clients.
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Fig.1 Schematic diagram of ST6GalNAc inhibitor development service. (CD BioGlyco)
Publication
Technology: PCR array analysis
Journal: Gastric Cancer
IF: 8.013
Published: 2016
Results: Regulation of ST6GalNAc I gene expression plays a decisive role in the growth and migration of gastric cancer cells. It regulates the gene expression of IGF-1 by activating the STAT5b pathway in cancer cells. By PCR array analysis, ST6GalNAc I mRNA was observed in all six gastric cancer cell lines, with MKN 45 expressing the first and MKN 74 cells the worst. In addition, the phosphorylation level of STAT5b was also affected by the ST6GalNAc I. By intraperitoneal injection in mice, ST6GalNAc I. significantly suppressed tumor metastasis and prolonged survival. ST6GalNAc I may be a target for peritoneal dissemination therapy in gastric cancer.
Fig.2 Suppression of ST6GalNAc I by siRNA inhibits cell invasion and migration in gastric cancer cell lines. (Tamura, et al., 2016)
Applications of ST6GalNAc Inhibitor
- ST6GalNAc inhibitors play a key role in treating pancreatic, colorectal, ovarian, and breast cancer-related metastasis.
- ST6GalNAc inhibitors regulate the gene expression of IGF-1 in gastric cancer cells by activating STAT5b and may be a potential target for metastatic gastric cancer therapy.
- ST6GalNAc inhibitors are the biomarkers of cancer cell invasion.
- The expression of the ST6GalNAc inhibitor is increased in direct proportion to the expression of the α series of gangliosides in breast cancer cells, promoting their ability to form brain metastases.
CD BioGlyco has a complete solution for Glycosylation Inhibitor Development. We have knowledgeable researchers to help our clients with every project. In addition, we offer professional Capping Modification Inhibitor Development services. Please feel free to contact us.
References
- Li, M.; et al. Integrative analysis of the ST6GALNAC family identifies GATA2-upregulated ST6GALNAC5 as an adverse prognostic biomarker promoting prostate cancer cell invasion. Cancer Cell Int. 2023, 23(1): 141.
- Tamura, F.; et al. RNAi-mediated gene silencing of ST6GalNAc I suppresses the metastatic potential in gastric cancer cells. Gastric Cancer. 2016, 19(1): 85-97.
- Yu, X.; et al. Silencing of ST6GalNAc I suppresses the proliferation, migration, and invasion of hepatocarcinoma cells through the PI3K/AKT/NF-κB pathway. Tumour Biol. 2016, 37(9): 12213-12221.
- Crespo, H.J.; et al. Dendritic cells: a spot on sialic acid. Front Immunol. 2013, 4: 491.
