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Fucosylationo fg lycansi mpactsamyriado f physiological and pathological processes. Inhibition of fucose expression emerges as ap otential therapeutic avenuef or example in cancer,inflammation, and infection. In this study,w ef ound that protected 2-fluorofucose 1phosphate efficiently inhibits cellular fucosylation with a four to seven times higher potencyt han knowni nhibitor 2FF,i ndependently of the anomeric stereochemistry.N ucleotides ugar analysisr evealed that both the a-a nd b-GDP-2FF anomers are formed insidet he cell. In conclusion, we developed A2FF1P and B2FF1P as potent new tools for studying the role of fucosylation in health and diseasea nd they are potential therapeutic candidates.
<a>Fucosylation
of glycans impacts a myriad of physiological and pathological processes. Inhibition
of fucose expression emerges as a potential therapeutic avenue for example in
cancer, inflammation, and infection. In this study, we found that protected 2-fluorofucose
1-phosphate efficiently inhibits cellular fucosylation with a four to seven
times higher potency than known inhibitor 2FF, independently of the anomeric
stereochemistry. Nucleotide sugar analysis revealed that both the α- and β-GDP-2FF anomers are
formed inside the cell. In conclusion, we developed A2FF1P and B2FF1P as potent
new tools for studying the role of fucosylation in health and disease</a> and they are potential therapeutic candidates.
Objective
To assess anti–cytosolic 5′‐nucleotidase 1A (anti–cN‐1A) autoantibodies in children with juvenile dermatomyositis (DM) and healthy controls, using 3 different methods of antibody detection, as well as verification of the results in an independent cohort.
Methods
Anti–cN‐1A reactivity was assessed in 34 Dutch juvenile DM patients and 20 healthy juvenile controls using the following methods: a commercially available full‐length cN‐1A enzyme‐linked immunosorbent assay (ELISA), a synthetic peptide ELISA, and immunoblotting with a lysate from cN‐1A–expressing HEK 293 cells. Sera from juvenile DM patients with active disease and those with disease in remission were analyzed. An independent British cohort of 110 juvenile DM patients and 43 healthy juvenile controls was assessed using an in‐house full‐length cN‐1A ELISA.
Results
Anti–cN‐1A reactivity was not present in sera from juvenile DM patients or healthy controls when tested with the commercially available full‐length cN‐1A ELISA or by immunoblotting, in either active disease or disease in remission. Additionally, in the British juvenile DM cohort, anti–cN‐1A reactivity was not detected. Three Dutch juvenile DM patients had weakly positive results for 1 of 3 synthetic cN‐1A peptides measured by ELISA.
Conclusion
Juvenile DM patients and young healthy individuals did not show anti–cN‐1A reactivity as assessed by different antibody detection techniques.
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