Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.4.99.6 (sialyltransferase)
 1,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sialyltransferase activities, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), in Colo 205 cells catalyze the transfer of sialic acid to the terminal galactose of GlcNc-- and GalNAc-containing glycolipid substrates, respectively. Competition kinetic studies with nLcOse4Cer and GM1 as substrates in a sialyltransferase assay show that these two activities are catalyzed by two different catalytic entities. The two enzymes were co-solubilized with taurochlorate and resolved by DEAE--Cibacron Blue--Sepharose column chromatography into two elution peaks. The column eluent with SAT-3 activity failed to transfer sialic acid to asialo alpha(1)-acid glycoprotein, indicating that this enzyme is different from the sialyltransferase (ST3N) that synthesizes NeuAc alpha 2-3Gal linkage in asparagine-linked oligosaccharides of glycoprotein. However, SAT-3 activity can be immunoprecipitated with a polyclonal antibody produced against a protein expressed in Escherichia coli as GST-fusion protein from an ECB cDNA homolog of an alpha 2-3 sialyltransferase SAT-3 or STZ) the has been cloned from human melanoma cell and human placenta. Thus a concentration-dependent decrease in the residual SAT-3 activity relative to SAT-4 activity was observed in the supernatant after precipitation of the immune complex. Expression of SAT-3 (STZ) cDNA was also detected in Colo 205 cell by RT-PCR, followed by sequence analysis of the RT-PCR product. Characterization of the catalytic reaction products of SAT-3 and SAT-4 with thin-layer chromatography, sialidase treatment, and binding to specific antibodies indicates that both SAT-3 and SAT-4 catalyze the formation of alpha 2-3 linkage between sialic acid and terminal galactose of glycolipid substrates.
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PMID:Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line. 861

9-O-Acetylation of sialic acids shows cell type-specific and developmentally regulated expression in various systems. In a given cell type, O-acetylation can also be specific to a particular type of glycoconjugate. It is assumed that this regulation is achieved by control of expression of specific 9-O-acetyltransferases. However, it has been difficult to test this hypothesis, as these enzymes have so far proven intractable to purification or molecular cloning. During a cloning attempt, we discovered that while polyoma T antigen-positive Chinese hamster ovary cells (CHO-Tag cells) do not normally express cell-surface 9-O-acetylation, they do so when transiently transfected with a cDNA encoding the lactosamine-specific alpha2-6-sialyltransferase (Galbeta1-4GlcNAc:alpha2-6-sialyltransferase (ST6Gal I); formerly ST6N). This phenomenon is reproducible by stable expression of ST6Gal I in parental CHO cells, but not upon transfection of the competing lactosamine-specific alpha2-3-sialyltransferase (Galbeta1-(3)4GlcNAc:alpha2-3-sialyltransferase; (ST6Gal III) formerly ST3N) into either cell type. Further analyses of stably transfected parental CHO-K1 cells indicated that expression of the ST6Gal I gene causes selective 9-O-acetylation of alpha2-6-linked sialic acid residues on N-linked oligosaccharides. In a similar manner, while the alpha2-3-linked sialic acid residue of the endogenous GM3 ganglioside of CHO cells is not O-acetylated, transfection of an alpha2-8-sialyltransferase (GM3:alpha2-8-sialyltransferase (ST8Sia I); formerly GD3 synthase) caused expression of 9-O-acetylation of the alpha2-8-linked sialic acid residues of newly synthesized GD3. These data indicate either that linkage-specific sialic acid O-acetyltransferase(s) are constitutively expressed in CHO cells or that expression of these enzymes is secondarily induced upon expression of certain sialyltransferases. The former explanation is supported by a low level of background 9-O-acetylation found in parental CHO-K1 cells and by the finding that O-acetylation is not induced when the ST6Gal I or ST8Sia I cDNAs are overexpressed in SV40 T antigen-expressing primate (COS) cells. Taken together, these results indicate that expression of sialic acid 9-O-acetylation can be regulated by the action of specific sialyltransferases that alter the predominant linkage of the terminal sialic acids found on specific classes of glycoconjugates.
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PMID:Linkage-specific action of endogenous sialic acid O-acetyltransferase in Chinese hamster ovary cells. 866 76

The adhesion of circulating cancer cells to vascular endothelium is an important step in the hematogenous metastasis of cancer. Until recently, it has been believed that carbohydrate antigens are expressed on cancer cells, and E-selectin is expressed on endothelial cells to effect this adhesion. We investigated the gene expression of fucosyl-transferase (Fuc-T) and sialyltransferase (ST), which are involved in the synthesis of sialyl Lewisx (s-Lex) in breast cancer by using Northern blot analysis. The concentration of s-Lex in the cancerous portion was increased, compared to that in the adjacent non-cancerous portion. A correlation was found between the concentration of s-Lex and the amount of Fuc-T VI message in 9 cases of breast cancer tissue. Expression of the Fuc-T III message was found in only one case who expressed s-Lea. No expression of the Fuc-T V or VII message was observed. There was no relationship between the concentration of s-Lex and the amount of ST3N and ST4 transcripts. Similar findings were obtained from an analysis using cell lines derived from human breast cancer. When Fuc-T VI gene was transfected to MCF-7 cells, the expression of s-Lex was markedly induced on MCF-7 cells, and the attachment of cancer cells to endothelial cells was enhanced. These findings suggest that Fuc-T VI is chiefly involved in the synthesis of s-Lex on breast cancer cells.
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PMID:Gene expression of fucosyl- and sialyl-transferases which synthesize sialyl Lewisx, the carbohydrate ligands for E-selectin, in human breast cancer. 953 43

Glycosylation is key posttranslational modification for membrane-bound and secreted proteins that can influence both the secondary structure and the function of the protein backbone. In order to investigate the effect of altered cellular glycosylation potential, we have generated a number of clonal cell lines over-expressing the alpha2,3(N) sialyltransferase enzyme (ST3N). In general, there was a decrease in total sialyltransferase (ST) enzyme activity in the clones transfected with the ST3N cDNA, with this decrease being inversely proportional to the quantity of the mRNA coding for the enzyme. The ST3N enzyme was, however, functional and there was an increase in both MAA lectin staining and the expression of polysialic acid, which is attached to the NCAM protein backbone primarily via an alpha2,3 linkage. These results suggest that the overexpression of a sialyltransferase may upset the sialylation potential of the cell.
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PMID:Overexpression of alpha2,3 sialyltransferase in neuroblastoma cells results in an upset in the glycosylation process. 1097 43

Bisubstrate-type sialyltransferase inhibitors 1/2a-e, having CMP-NeuAc and N-acetyllactosamine (or lactose) moieties connected by an alkanedithiol linker, were synthesized systematically. A uniform synthetic strategy was adopted that consists of consecutive couplings of three components (N-acetyllactosamine or lactose, sialic acid, and CMP), followed by oxidation. Due to the sensitivity of the compounds under alkaline conditions, final deprotection required careful monitoring by (1)H NMR. The inhibitory activities of 1/2a-e toward ST6N and ST3N indicated that both the structure of the acceptor moiety and the distance between donor and acceptor moieties were important.
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PMID:Systematic syntheses and inhibitory activities of bisubstrate-type inhibitors of sialyltransferases. 1283 52