ArticleThe Journal of biological chemistry2011
Sialylation of the Fas death receptor by ST6Gal-I provides protection against Fas-mediated apoptosis in colon carcinoma cells.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.
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Who cites it
132 citing papers in PubMed, 222 citations in OpenAlex.
- Aberrant sialylation in cancer: From molecular mechanisms to potential therapeutics.Genes & diseases · 2026Review
- Targeting Siglec-engaging immunosuppressive sialoglycans to suppress prostate cancer bone metastasis.British journal of cancer · 2026Article
- Review
- Sweet Surprises: Decoding Tumor-Associated Glycosylation in Cancer Progression and Therapeutic Potential.Cells · 2026Review
- Downregulation of sialyl-transferases and their role in malignant meningioma cells.Biomedical reports · 2026Article
- Sialylation Inhibition Impairs Migration and Promotes Adhesion of GBM Cells.International journal of molecular sciences · 2025Article
- A Potent Oral Sialylation Inhibitor Augments the Immunotherapy in Pancreatic Ductal Adenocarcinoma.ACS central science · 2025Article
- Glycosylation in kidney diseases.Precision clinical medicine · 2025Review
- Multi-omics reveals that ST6GAL1 promotes colorectal cancer progression through LGALS3BP sialylation.Biomolecules & biomedicine · 2025Article
- The Tumour Glyco-Code: Sialylation as a Mediator of Stromal Cell Immunosuppression in the Tumour Microenvironment.European journal of immunology · 2025Review
- Aberrant Sialylation in Ovarian Cancer: Orchestrating Progression, Metastasis, and Therapeutic Hurdles.Current medical science · 2025Review
- AcetylatedFrontiers in oncology · 2025Article
- Swainsonine Protects Human Thyrocytes from Fas-Induced Apoptosis: In vitro Study on Nthy-Ori 3-1 Cell Line.Journal of inflammation research · 2025Article
- Anticancer approach by targeted activation of a global inhibitor of sialyltransferases with acrolein.Chemical science · 2024Article
- Specific sialylation of N-glycans and its novel regulatory mechanism.Glycoconjugate journal · 2024Review
- ST6GAL1 is associated with poor response to chemoradiation in rectal cancer.Neoplasia (New York, N.Y.) · 2024Article
- Review
- When a negative (charge) is not a positive: sialylation and its role in cancer mechanics and progression.Frontiers in oncology · 2024Review
- Role of ST6GAL1 in Thyroid Cancers: Insights from Tissue Analysis and Genomic Datasets.International journal of molecular sciences · 2023Article
- ST6GAL1 sialyltransferase promotes acinar to ductal metaplasia and pancreatic cancer progression.JCI insight · 2023Article
72 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The glycosyltransferase, ST6Gal-I, adds sialic acid in an α2-6 linkage to the N-glycans of membrane and secreted glycoproteins. Up-regulation of ST6Gal-I occurs in many cancers, including colon carcinoma, and correlates with metastasis and poor prognosis. However, mechanisms by which ST6Gal-I facilitates tumor progression remain poorly understood due to limited knowledge of enzyme substrates. Herein we identify the death receptor, Fas (CD95), as an ST6Gal-I substrate, and show that α2-6 sialylation of Fas confers protection against Fas-mediated apoptosis. Intriguingly, differences in ST6Gal-I activity do not affect the function of DR4 or DR5 death receptors upon treatment with TRAIL, implicating a selective effect of ST6Gal-I on the Fas receptor. Using ST6Gal-I knockdown and forced overexpression colon carcinoma cell models, we find that α2-6 sialylation of Fas prevents apoptosis stimulated by FasL as well as the Fas-activating antibody, CH11, as evidenced by decreased activation of caspases 8 and 3. We also show that α2-6 sialylation of Fas does not alter the binding of CH11, but rather inhibits the capacity of Fas to induce apoptosis by blocking the association of FADD with Fas cytoplasmic tails, an event that initiates death-inducing signaling complex formation. Furthermore, α2-6 sialylation of Fas inhibits Fas internalization, which is required for apoptotic signaling. Although dysregulated Fas activity is a well known mechanism through which tumors evade apoptosis, the current study is the first to link Fas insensitivity to the actions of a specific sialyltransferase. This finding establishes a new paradigm by which death receptor function is impaired for the self-protection of tumors against apoptosis.
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