Poly-N-acetyllactosamine epitope on basigin (CD147) and CD98 (No widely accepted single abbreviation exists for this glycan+protein epitope. Related abbreviations include CD147 for basigin/EMMPRIN, CD98 for SLC3A2, and sometimes poly-N-acetyllactosamine is abbreviated as polyLacNAc.)

Poly-N-acetyllactosamine is a linear or branched glycan (carbohydrate) chain modification consisting of repeating N-acetyllactosamine (LacNAc, Galβ1-4GlcNAcβ1-3) units. On cell surface glycoproteins, especially basigin (CD147) and CD98, it is produced by the branching actions of glycosyltransferases such as GnT-V. Highly branched, poly-N-acetyllactosamine-rich forms of CD147 are prevalent on tumor cells and are associated with enhanced protein stability, membrane trafficking, and protein-protein interactions crucial for tumor progression, metabolic adaptation, and immune cell interaction. CD147 interacts closely with monocarboxylate transporters and CD98, forming complexes necessary for nutrient and metabolite transport, immune regulation, and signal transduction. The presence and abundance of poly-N-acetyllactosamine epitopes on CD147 (and potentially CD98) are key determinants for cellular function and represent validated therapeutic targets and biomarkers, especially in oncology.

Other names

Poly-N-acetyllactosamine (polyLacNAc) epitopeβ1,6-branched polylactosamine on CD147EMMPRIN (for CD147)Basigin (for CD147)SLC3A2 (for CD98)

Antibody blockade: Anti-CD147 antibodies can inhibit MMP induction, tumor invasion, or virus entry by blocking protein interactions or masking glycan-dependent epitopes. Transporter inhibition: Disruption of the CD147/MCT or CD98/amino acid transporter complex impedes metabolic adaptation of tumor cells. Glycosylation modulation: Inhibitors of glycosyltransferases (e.g., GnT-V inhibitors) could reduce poly-N-acetyllactosamine epitopes, potentially impacting the function and stability of CD147 or CD98.