Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.4.99.7 (sialyltransferase)
 1,534 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

CDw75, a B lymphocyte surface antigen, is a sialylated carbohydrate epitope, which is generated by the enzyme beta galactosyl alpha 2,6 sialyltransferase (Sia-T1). In colon carcinomas, although higher levels of Sia-T1 has been described and found to be correlated with metastatic potential of tumor cells, the expression of CDw75 antigen still remains unknown. To address this issue, we investigated immunohistochemically CDw75 antigen expression in 195 colorectal adenocarcinomas and their nodal metastases. The correlation between CDw75 antigen expression with selected clinicopathologic variables was analyzed by using Chi-square and Fisher s exact tests. Positive staining was observed in 101 cases. Non-neoplastic mucosa was negative consistently. The frequency of positivity was decreased according to the degree of differentiation (p<0.001). Antigen expression was found to be associated with deeper penetration (p<0.006), positive lymph nodes (p<0.001), distant metastases (p<0.006) and advanced stage (p<0.001). Same relationships were detected in well and moderately differentiated tumors when CDw75 immunoreactivity was evaluated in each histologic grade separately. Our findings indicate that CDw75 antigen expression may be a good indicator of the biological aggressiveness of colorectal adenocarcinomas especially in tumors with well and moderately differentiated morphology.
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PMID:Clinicopathologic evaluation of CDw75 antigen expression in colorectal adenocarcinomas. 1251 97

Changes in cell surface glycosylation are common modifications that occur during oncogenesis, leading to the over-expression of tumour-associated carbohydrate antigens (TACA). Most of these antigens are sialylated and the increase of sialylation is a well-known feature of transformed cells. In breast cancer, expression of TACA such as sialyl-Lewis(x) or sialyl-Tn is usually associated with a poor prognosis and a decreased overall survival of patients. However, the specific role of these sialylated antigens in breast tumour development and aggressiveness is not clearly understood. These glycosylation changes result from the modification of the expression of genes encoding specific glycosyltransferases involved in glycan biosynthesis and the level of expression of sialyltransferase genes has been proposed to be a prognostic marker for the follow-up of breast cancer patients. Several human cellular models have been developed in order to explain the mechanisms by which carbohydrate antigens can reinforce breast cancer progression and aggressiveness. TACA expression is associated with changes in cell adhesion, migration, proliferation and tumour growth. In addition, recent data on glycolipid biosynthesis indicate an important role of G(D3) synthase expression in breast cancer progression. The aim of this review is to summarize our current knowledge of sialylation changes that occur in breast cancer and to describe the cellular models developed to analyze the consequences of these changes on disease progression and aggressiveness.
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PMID:Consequences of the expression of sialylated antigens in breast cancer. 2023 Oct 16

ST6GalNAc-I, the sialyltransferase responsible for sialyl-Tn (sTn) synthesis, has been previously reported to be positively associated with cancer aggressiveness. Here we describe a novel sTn-dependent mechanism for chemotherapeutic resistance. We show that sTn protects cancer cells against chemotherapeutic-induced cell death by decreasing the interaction of cell surface glycan receptors with galectin-3 and increasing its intracellular accumulation. Moreover, exogenously added galectin-3 potentiated the chemotherapeutics-induced cytotoxicity in sTn non-expressing cells, while sTn overexpressing cells were protected. We also found that the expression of sTn was associated with a reduction in galectin-3-binding sites in human gastric samples tumors. ST6GalNAc-I knockdown restored galectin-3-binding sites on the cell surface and chemotherapeutics sensibility. Our results clearly demonstrate that an interruption of O-glycans extension caused by ST6GalNAc-I enzymatic activity leads to tumor cells resistance to chemotherapeutic drugs, highlighting the need for the development of novel strategies to target galectin-3 and/or ST6GalNAc-I.
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PMID:O-glycan sialylation alters galectin-3 subcellular localization and decreases chemotherapy sensitivity in gastric cancer. 2783 77