- 期刊
Altered Sialylation and Its Roles in Gynecologic Cancers
並列摘要
Alterations on the cell surface of the oligosaccharide portion of glycoconjugates, including glycoproteins and glycolipids, are thought to play a role in tumor transformation and progression. The recent report published in the Journal of Cancer Molecules (Wang PH 2005) highlights the general concept about sialic acids (SAs), sialyltransferases (STs), and the relationship between altered sialylation and cancer transformation, progression, and metastasis. The SAs are acidic monosaccharides typically found at the outermost ends of the oligosaccharide chains of glycoconjugates. ST catalyzes the incorporation of SA to the carbohydrate group of glycoconjugates. The human genome encodes probably more than 20 different STs involved in the biosynthesis of sialylated glycoconjugates but up to date only 20 different human ST cDNAs have been cloned and characterized. Each of ST genes is differentially expressed in a tissue, cell type, and stage-specific manner to regulate the sialylation pattern of cells, with resultant complicating processes not only for research but also for future application. In human cancer, alterations of sialylated glycan structures are related to tumor behaviors; this may depend on altered regulation of one or more ST genes. However, several distinct ST enzymes arising from different unique genes transfer SA residues in the same linkage onto the same acceptor; it is difficult to precisely determine which ST is really involved in the observed phenotype. Therefore, to study the roles of SA and ST is still an attractive field in cancer research. In this paper, the recent works addressing the altered sialylation in cancers of the cervix, ovary and breast are systemically reviewed and highlighted the value in future application.