| First Author | Tanida S | Year | 2014 |
| Journal | Biochim Biophys Acta | Volume | 1840 |
| Issue | 6 | Pages | 1790-7 |
| PubMed ID | 24561267 | Mgi Jnum | J:211579 |
| Mgi Id | MGI:5575699 | Doi | 10.1016/j.bbagen.2014.02.008 |
| Citation | Tanida S, et al. (2014) Galectin-3 binds to MUC1-N-terminal domain and triggers recruitment of beta-catenin in MUC1-expressing mouse 3T3 cells. Biochim Biophys Acta 1840(6):1790-7 |
| abstractText | BACKGROUND: Galectin-3 is expressed in a variety of tumors and its expression level is related with tumor progression. Aberrant expression of MUC1 in various tumors is also associated with a poor prognosis. It has been reported that MUC1 is a natural ligand of galectin-3. METHODS: A stable MUC1 transfectant was produced by introducing MUC1 cDNA into mouse 3T3 fibroblasts (MUC1/3T3 cells). MUC1 was prepared from MUC1/3T3 cells; MUC1-N-terminal domain (MUC1-ND) and -C-terminal domain (MUC1-CD) were separated by CsCl ultracentrifugation, and then the galectin-3-binding domain was determined by co-immuniprecipitation assay. After ligation of galectin-3 to 3T3/MUC1 cells, MUC1-CD was immunoprecipitated from the cell lysate. The immunoprecipitate was subjected to SDS-PAGE and Western blotting, followed by detection of co-immunoprecipitated beta-catenin. RESULTS: Galectin-3 binds to the N-terminal domain of MUC1 but not to the C-terminal one. Galectin-3 present on the cell surface increased with the expression of MUC1 and is colocalized with MUC1. It should be noted that beta-catenin was detected in the immunoprecipitate with anti-MUC1-CD Ab from a lysate of galectin-3-treated 3T3/MUC1 cells. CONCLUSIONS: Galectin-3 binds to MUC1-ND and triggers MUC1-mediated signaling in 3T3/MUC1 cells, leading to recruitment of beta-catenin to MUC1-CD. GENERAL SIGNIFICANCE: This signaling may be another MUC1-mediated pathway and function in parallel with a growth factor-dependent MUC1-mediated pathway. |
