英文摘要 |
Altered glycosylation is found in all cancer cells, compared with normal cells. Sialic acid might be one of the most important molecules, since it is located on the terminal end of various kinds of oligosaccharides. Although this glycosylation of protein contributes to the half-life of circulating proteins, recent evidence shows it also contributes to the interaction between the cells. We found that overexpression of α 2,6-linked glycosylation and suppression of α 2,3-linked glycosylation in cervical cancer cells compared with normal cervix; however, when metastases of the cervical cancers occur, continuous overexpression of α 2,6-linked glycosylation but reverse overexpression of α 2,3-linked glycosylation is found in the cervical cancers, supposing that dynamic alternation of glycosylation might be important for tumor invasion and metastases. |