Aberrantly glycosylated Mucin 1 (MUC1)

Mucin-1 (MUC1) is a large, transmembrane, heavily O-glycosylated glycoprotein expressed on the apical surface of most epithelial cells. In healthy cells, MUC1 protects and lubricates tissue surfaces against environmental insults. In various carcinomas, MUC1 expression is upregulated, and its glycosylation becomes aberrant—glycan chains are truncated or altered, exposing core protein epitopes not normally present on healthy tissue. These changes play critical roles in tumor progression by modulating cell signaling (via EGFR, β-catenin, ERα interactions), cell adhesion, drug resistance, and immune evasion. Aberrantly glycosylated MUC1 is a clinically valuable target for cancer diagnostics, therapeutics (including antibody drugs and vaccines), and is central to the biology of tumor microenvironment remodeling, metastasis, and therapy resistance[1][2][3][4][5][6][7][8].

Other names

Polymorphic epithelial mucin (PEM)MUC1epithelial mucin-1mucin 1 glycoproteintumor-associated MUC1

Inhibition of MUC1 glycosylation to enhance drug penetration/drug efficacy. MUC1-specific antibody/immune targeting for tumor cell killing. Therapeutic vaccines targeting tumor-associated MUC1 antigens.