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Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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A novel approach to decrease sialic acid expression in cells by a C-3-modified N-acetylmannosamine.

Paul R Wratil1, Stephan Rigol2, Barbara Solecka3

  • 1Institut für Laboratoriumsmedizin, Klinische Chemie, und Pathobiochemie, Charité-Universitätsmedizin Berlin, Campus Benjamin Franklin, Arnimallee 22, D-14195 Berlin-Dahlem.

The Journal of Biological Chemistry
|October 4, 2014
PubMed
Summary

A novel compound, 2-acetylamino-2-deoxy-3-O-methyl-D-mannose, effectively reduces cell surface sialylation by inhibiting the key enzyme in sialic acid biosynthesis. This discovery offers potential therapeutic applications in cancer and infectious diseases.

Keywords:
Enzyme InhibitorFlow CytometryGlycosylation InhibitorHigh-performance Liquid Chromatography (HPLC)Sialic AcidSurface Plasmon Resonance (SPR)

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Sialic acid, located on cell surfaces, plays critical roles in cell functions including immune regulation and tumor evasion.
  • Inhibiting cell surface sialylation presents a promising therapeutic strategy for cancer, immune disorders, and infectious diseases.

Purpose of the Study:

  • To evaluate novel C-3 modified N-acetylmannosamine analogs as potential inhibitors of cell surface sialylation.
  • To investigate the mechanism of action and specificity of the most effective inhibitor.

Main Methods:

  • Synthesis and testing of four C-3 modified N-acetylmannosamine analogs.
  • Flow cytometry and enzyme-linked lectin assays to quantify cell surface sialylation.
  • High-performance liquid chromatography to measure intracellular sialic acid levels.
  • Surface plasmon resonance to determine binding kinetics and specificity against target enzymes.

Main Results:

  • Peracetylated 2-acetylamino-2-deoxy-3-O-methyl-D-mannose significantly decreased cell surface sialylation in Jurkat cells by up to 80% in a dose-dependent manner.
  • This compound reduced both membrane-bound and cytosolic sialic acid concentrations.
  • Evidence suggests inhibition of the bifunctional enzyme UDP-GlcNAc-2-epimerase/ManNAc kinase, specifically its human ManNAc kinase domain.
  • High specificity for human N-acetylmannosamine kinase (MNK) was confirmed, with minimal activity against related kinases.

Conclusions:

  • 2-Acetylamino-2-deoxy-3-O-methyl-D-mannose is a novel inhibitor targeting the de novo biosynthesis of sialic acid.
  • This compound represents a new class of sialic acid expression inhibitors with potential therapeutic applications.