ArticleGlycoconjugate journal1999
Overexpression of alpha2,3 sialyltransferase in neuroblastoma cells results in an upset in the glycosylation process.
Article in Glycoconjugate journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Functional Consequences of Differential O-glycosylation of MUC1, MUC4, and MUC16 (Downstream Effects on Signaling).Biomolecules · 2016Review
- Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain.Glycoconjugate journal · 2004Article
- Retinoic acid induction of sialyltransferase activity in neuroblastoma cells of differing sialylation potentials.Glycoconjugate journal · 2000Article
- Achievements and challenges of sialic acid research.Glycoconjugate journalReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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