Mucin 1 glycoprotein (MUC1)

Mucin 1 glycoprotein (MUC1) is a type I transmembrane protein characterized by a large, heavily O-glycosylated extracellular domain containing variable numbers of 20 amino acid tandem repeats (VNTR)[1][2][3]. It forms a protective anti-adhesive barrier on the surface of epithelial cells in numerous organs, contributing to lubrication and resistance to infection[3]. The cytoplasmic tail participates in cell signaling, interacting with multiple kinase pathways (EGFR, MET, Src, PKC, Abl, among others)[1]. Aberrant overexpression and glycosylation of MUC1 are hallmarks of many epithelial cancers, where it promotes tumor progression, resistance to apoptosis, invasion, metastasis, and resistance to conventional therapies[1][2]. MUC1 serves both as a therapeutic target for antibodies and cancer vaccines, and as a biomarker (CA15-3) for disease monitoring. Isoform and glycan heterogeneity, as well as expression in normal tissues, present challenges for therapeutic exploitation[2].

Other names

episialinPEMH23AgEMACA15-3MCA

Drugs targeting MUC1 primarily work through direct binding and inhibition of MUC1 expressing cells (e.g., antibodies, vaccines), immunomodulation by targeting MUC1 on cancer or infected cells, inducing anti-MUC1 cytotoxic T-cell responses, and inhibition of cell signaling pathways, thereby suppressing oncogenic activity.