Purpose:
@EN Mucinous colorectal cancers have a poorer prognosis than which colorectal cancer produce low amount of mucin, but the exact mechanism is not well understood. The present study was undertaken to elucidate the exact mechanism of invasion and
metastasis of high mucin producing colon cancer cells using mucin glycosylation inhibitor, benzyl-α-N-acetylgalactosamine.
@ES Materials and Methods:
@EN To evaluate the effect of glycosylated mucin on invasion and metastasis, in vitro invasion, metalloproteinases(MMPs) activity, cell-matrix protein binding, cell-cell aggregation, as well as endothelial leukocyte adhesion molecule(ELAM-1)
binding and
cell surface expression of various mucin related antigens were analyzed.
@ES Results:
@EN MMPs activity in conditioned medium and invasion of ECM-coated porous filters by benzyl-a-GalNAc treated HM7 cells were decreased. There was no difference between control and treated HM7 cells in terms of matrix protein binding assay, but
treated
HM7 cells showed higher homotypic cell adhesion. The binding activity of treated HM7 cells to ELAM-1 was significantly decreased and fixed cell binding of MoAb SNH-3, 19-9(specific for sialyl-Lewis X and sialyl-Lewis A) were also significantly
decreased.
@ES Conclusion:
@EN These results suggest that glycosylated mucin modulates ELAM-1 binding, MMPs activity and homotypic cell adhesion, therefore enhance invasive and metastatic properties of human colon cancer cells.
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