Customer Spotlight: Radiotherapy-Induced Sialyation and Immune Response Changes in Pancreatic Cancer
“Vector Laboratories’ lectins provide an extremely consistent and cost-effective way to monitor cell-surface sialylation by flow cytometry, meaning we have the confidence that any observed changes reflect the biology rather than variability in an assay reagent.”
That’s how Dr. Miya Paserba and Dr. Deepak Nagrath, of the Department of Biomedical Engineering at the University of Michigan, Ann Arbor, describe using MAL II and SNA lectins in their research on pancreatic ductal adenocarcinoma (PDAC).
Their lab studies how radiotherapy-induced changes in sialic acid synthesis alter cell-surface sialylation and anti-tumor immune response. By combining metabolic interventions with metabolomics, lectin flow cytometry, and functional immune assays, the team is working to identify therapeutic targets that could make radiotherapy more effective for patients with PDAC.
MAL II and SNA, which bind α2,3- and α2,6-linked sialic acids respectively, give the lab a way to measure cell-surface sialylation patterns by flow cytometry, bridging metabolic changes inside the cell to phenotypic changes at the surface.
“Without MAL II and SNA, we would not have a straightforward way to connect metabolic pathway activity to a cell-surface phenotype,” the researchers said. Relative to technically intensive approaches like glycomics, lectin flow cytometry gives the researchers higher-throughput, quantitative results at the single-cell level.
Going forward, the lab plans to keep MAL II and SNA as core tools in their workflow, and to bring in the Glysite™ Scout Kit to profile broader glycosylation changes in PDAC tissue samples over the course of treatment.
B. Pancreatic ductal adenocarcinoma-derived cancer-associated fibroblasts demonstrate an increase in 2,3- and 2,6-sialyation after exposure to 4Gy ionizing radiation, which lasts up to 7 days.
B. Pancreatic ductal adenocarcinoma-derived cancer-associated fibroblasts demonstrate an increase in 2,3- and 2,6-sialyation after exposure to 4Gy ionizing radiation, which lasts up to 7 days. Data presented as mean +/- SE, analyzed using two-way ANOVA with Dunnett’s multiple comparison test (n=3).
Seeing Protein Glycosylation in Cancer Research
Glycosylation is one of the most common post-translational modifications (PTMs) and impacts protein function, stability, and cellular communication. Altered glycosylation is implicated in cancer initiation, progression, and treatment. The heterogeneity of glycosylation and lack of tailor-made tools make adding the dimension of glycosylation to cancer studies difficult, but Vector Laboratories’ suite of reliable glycobiology tools makes this overlooked PTM accessible to researchers of at all levels of glycobiology experience.
The following articles from the Vector Laboratories blog highlight how adding protein glycosylation analysis to cancer research deepens understanding.
- The Overlooked PTM: Making Glycosylation More Accessible to Researchers
- Revisiting Colon Cancer Metastasis Through a Glycobiology Lens
- Glycosylation in the Alzheimer’s Brain: Visualizing New Paths to Diagnosis and Therapy
- Advancing Colorectal Cancer Research with Biomarker-Driven Tools
- A New Focus for Breast Cancer: Protein Glycosylation’s Emerging Role
- Glycans and Immune Checkpoints: Revealing Hidden Influences on Cancer Immunotherapy
