The speculations on the role of MUC1, a substance which is overexpressed in glandular
cancer cells, on the metastatic potential of such cells are rooted in data that seem to indicate that cell malignization correlates with a change from the apical localization of
mucin MUC1 to a peripheral one. Nonetheless, the role of MUC1 in
cancer metastasizing remains far from clear. The major hurdle remains the absence of adequate cell models. The aim of the present study was to create cell models that present different fragments of the human
mucin MUC1 extracellular domain on their surface. Genetic constructions were generated on the basis of the plasmid vector pEGFP-N3. These constructions contain fusion genes coding for chimeric
proteins composed of different combinations of
mucin MUC1 functional domains and identification markers (FLAG-
epitope, located at the N-terminus, and EGFP, located at the C-terminus of the chimeric
proteins). These constructions were used for a stable transformation of HT-29 human
cancer cells. The transformants obtained were characterized by flow cytometry. The low expression level of endogenous
mucin MUC1 and the high expression level of
recombinant proteins were confirmed by real-time PCR. The microscopic examination of the transformed cells confirmed the membrane localization of the fusion
proteins. The resulting cell models could be used to investigate the role of the
mucin MUC1 domains in
cancer cell metastasizing. The obtained cells are used as an applicable model of MUC1-expressing
cancers and might be used to study the role of different functional fragments of
mucin MUC1 in metastasizing.