Publications by authors named "Benedicte Samyn-Petit"
The Sialyl-Tn antigen (Neu5Acalpha2-6GalNAc-O-Ser/Thr) is highly expressed in several human carcinomas and is associated with carcinoma aggressiveness and poor prognosis. We characterized two human sialyltransferases, CMP-Neu5Ac:GalNAc-R alpha2,6-sialyltransferase (ST6GalNAc)-I and ST6GalNAc-II, that are candidate enzymes for Sialyl-Tn synthases. We expressed soluble recombinant hST6GalNAc-I and hST6GalNAc-II and characterized the substrate specificity of both enzymes toward a panel of glycopeptides, glycoproteins, and other synthetic glycoconjugates.
View Article and Find Full Text PDFWe have compared the site-by-site N-glycosylation status of human lactoferrin (Lf) produced in maize, a monocotyledon, and in tobacco, used as a model dicotyledon. Maize and tobacco plants were stably transformed and recombinant Lf was purified from both seeds and leaves. N-glycopeptides were generated by trypsin digestion of recombinant Lf and purified by reverse-phase HPLC.
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- The study identified a new sialyltransferase gene, ST6Gal II, on chromosome 2 by using the human CMP-sialic acid:beta-galactoside alpha-2,6-sialyltransferase cDNA as a probe.
- The genetic analysis revealed that ST6Gal II is distinct from other known sialyltransferases and shares similarities with hST6Gal I, exhibiting 48% identity.
- Enzymatic assays demonstrated that ST6Gal II has a preference for a specific disaccharide substrate and is primarily expressed in the brain, unlike ST6Gal I, which is found throughout various tissues.