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- W1897052165 abstract "An elevation of β‐galactoside α2,6‐sialyltransferase (ST6Gal.I) enzyme activity and an increased α2,6‐sialylation of cell membranes are among the most prominent glycosylation changes associated with colon cancer; both modifications correlate with a worse prognosis. In our previous studies, we have frequently observed a discrepancy between the ST6Gal.I level within a colon cancer sample or cell line and the respective level of reactivity with the α2,6‐sialyl‐specific lectin from Sambucus nigra (SNA). In this study, we have investigated quantitatively the biosynthesis of the sialyl‐α2,6‐lactosaminyl epitope in two colon cancer cell types expressing the ST6Gal.I cDNA under the control of a constitutive promoter. By measuring the amount of ST6Gal.I mRNA using competitive RT‐PCR, the expression of α2,6‐sialylated lactosaminic structures with SNA and anti‐CDw75 Ig, and the presence of unsubstituted lactosaminic termini by Erythrina cristagalli lectin, we reached the following conclusions: (a) a high proportion of the cell surface lactosaminic termini remains unsubstituted, even in the presence of a very high ST6Gal.I activity. This proportion is strongly dependent on the cell type; (b) ST6Gal.I‐transfected colon cancer cells do not express the CDw75 epitope; (c) the level of ST6Gal.I enzyme activity only partially correlates with the mRNA level; (d) despite the control by a constitutive promoter, the ST6Gal.I mRNA is not constantly expressed over time; and (e) a very large portion of the enzyme molecules is secreted in the extracellular milieu. These results indicate that post‐transcriptional and post‐translational mechanisms play a pivotal role in the control of α2,6‐sialylation in colon cancer cells." @default.
- W1897052165 created "2016-06-24" @default.
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- W1897052165 date "2001-11-15" @default.
- W1897052165 modified "2023-10-17" @default.
- W1897052165 title "Biosynthesis of the cancer-related sialyl-α2,6-lactosaminyl epitope in colon cancer cell lines expressing β-galactoside α2,6-sialyltransferase under a constitutive promoter" @default.
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- W1897052165 doi "https://doi.org/10.1046/j.0014-2956.2001.02536.x" @default.
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