Aberrant glycosylation is a common feature in most cancers and is associated with tumor-associated antigens. While there has been debate about whether aberrant glycosylation is a cause or a result of cancer, recent studies suggest it is a result of oncogenic transformation and plays a key role in invasion and metastasis. Glycosylation significantly influences tumor cell behavior, yet this area has received limited attention from cell biologists due to its complexity compared to other cancer-related mechanisms. The study by Kakugawa et al. highlights the role of ganglioside-specific sialidase Neu3 in colorectal cancer, leading to increased lactosylceramide (Lac-cer), which inhibits apoptosis by increasing Bcl-2 and decreasing caspase activity. This suggests that desialylated glycosphingolipid (GSL) core structures may influence tumor progression. However, the exact mechanisms by which specific glycosyl epitopes induce invasive and metastatic phenotypes remain unclear. Glycosylation patterns are closely linked to various cancer phenotypes, including apoptosis, motility, EGF receptor tyrosine kinase, angiogenesis, and adhesion to the extracellular matrix. For example, GM3 inhibits cell motility and EGF receptor activity, while Lac-cer inhibits apoptosis. The balance between different glycosyltransferases, such as GnT-V and GnT-III, determines the expression of glycosyl epitopes that influence metastasis. GnT-V promotes metastasis by stabilizing matriptase, while GnT-III has an antimetastatic effect. Other glycosylation changes, such as those involving SLe^x and SLe^a, are associated with tumor cell adhesion to endothelial cells and may influence metastasis. Additionally, siglecs and selectin epitopes play roles in cancer cell adhesion and progression. The study emphasizes the importance of understanding glycosylation in cancer, as it could lead to new therapeutic targets for antitumor drugs. The complex interplay between glycosylation and cancer progression remains an important area for future research.Aberrant glycosylation is a common feature in most cancers and is associated with tumor-associated antigens. While there has been debate about whether aberrant glycosylation is a cause or a result of cancer, recent studies suggest it is a result of oncogenic transformation and plays a key role in invasion and metastasis. Glycosylation significantly influences tumor cell behavior, yet this area has received limited attention from cell biologists due to its complexity compared to other cancer-related mechanisms. The study by Kakugawa et al. highlights the role of ganglioside-specific sialidase Neu3 in colorectal cancer, leading to increased lactosylceramide (Lac-cer), which inhibits apoptosis by increasing Bcl-2 and decreasing caspase activity. This suggests that desialylated glycosphingolipid (GSL) core structures may influence tumor progression. However, the exact mechanisms by which specific glycosyl epitopes induce invasive and metastatic phenotypes remain unclear. Glycosylation patterns are closely linked to various cancer phenotypes, including apoptosis, motility, EGF receptor tyrosine kinase, angiogenesis, and adhesion to the extracellular matrix. For example, GM3 inhibits cell motility and EGF receptor activity, while Lac-cer inhibits apoptosis. The balance between different glycosyltransferases, such as GnT-V and GnT-III, determines the expression of glycosyl epitopes that influence metastasis. GnT-V promotes metastasis by stabilizing matriptase, while GnT-III has an antimetastatic effect. Other glycosylation changes, such as those involving SLe^x and SLe^a, are associated with tumor cell adhesion to endothelial cells and may influence metastasis. Additionally, siglecs and selectin epitopes play roles in cancer cell adhesion and progression. The study emphasizes the importance of understanding glycosylation in cancer, as it could lead to new therapeutic targets for antitumor drugs. The complex interplay between glycosylation and cancer progression remains an important area for future research.