Identification of glycosylation-related changes in migratory and mechanical properties of bladder cancer cells

Glycosylation, a fundamental posttranslational modification, is crucial in cancer progression. Aberrant glycosylation patterns in tumor cells alter their interactions with the extracellular matrix (ECM), facilitating invasion and metastasis. Lectins are carbohydrate-binding proteins that selectively recognize these modifications, making them valuable tools for cancer detection. However, their impact on cancer cell behavior remains insufficiently explored. In this study, we examined the response of bladder cancers (non-malignant HCV29, non-invasive HT1376, and invasive T24 cancer cells) to surfaces coated with the lectins (Dolichosbiflorus agglutinin (DBA), Lensculinaris agglutinin (LCA), Phaseolus vulgaris leucoagglutinin (PHA-L), and Wheatgerm agglutinin (WGA)), using atomic force microscopy (AFM), cell imaging, and proliferation and migration assays. Our findings indicate that lectin coatings significantly influenced cancer cell proliferation and migration in a lectin-dependent manner. Notably, WGA induced the most pronounced effects, accelerating proliferation while simultaneously reducing migration, particularly in the invasive T24 cell line. Similarly, PHA-L increased proliferation. These results highlight the dual role of lectins as diagnostic markers and potential modulators of cancer cell behavior. While lectin-based biosensors offer promising tools for cancer detection, their influence on cell properties must be carefully considered to ensure reliable diagnostics. This study underscores the need for further research into the functional consequences of lectin-glycan interactions in cancer detection. Lectins, being beneficial for biosensing, may modulate cell behavior (as our results show), which potentially interferes with diagnostic capabilities.