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Sialyltransferase family members and cervix squamous cell carcinoma
1Department of Obstetrics and Gynecology, Taipei Veterans General Hospital, Department of Medicine, Cheng Hsin Rehabilitation Center, Institute of Clinical Medicine & Biochemistry National Yang-Ming University, Taipei, Taiwan
*Corresponding Author(s): P-H. WANG E-mail:
Sialic acids including a number of their derivatives are ubiquitous at the terminal positions of the oligosaccharides of glycoproteins. The transfer of sialic acids from cystidine-5-monophospho-N-acetylneuraminic acid (CMP-NeuAc) to the terminal position of the carbohydrate group of glycoproteins and glycolipids is catalyzed by a family of sialyltransferases (STs). There is a large body of evidence to suggest that tumor cells have altered surface properties from their normal counterparts, and that these changes are partially due to altered sialo-glycoconjugates expressed on the plasma membrane and that altered sialylation (change in glycoprotein expression), which occurs during certain pathological processes, such as oncogenic transformation, tumor metastases, and invasion, is associated with enhanced ST activity. In this report we attempt to review the important findings in studing sialyltransferases of cervix squamous cell carcinoma.
Prognosis; Sialyltransferase; Squamous cell carcinoma of the cervix
C. L. Chen,W. L. Lee,Y. C. Tsai,C. C. Yuan,H. T. Ng,P.H. Wang. Sialyltransferase family members and cervix squamous cell carcinoma. European Journal of Gynaecological Oncology. 2002. 23(6);514-518.
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