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O-Glycosylation of the Mucin Type

  • Franz-Georg Hanisch
Published/Copyright: June 1, 2005
Biological Chemistry
From the journal Volume 382 Issue 2

Abstract

While only about ten percent of the databank entries are defined as glycoproteins, it has been estimated recently that more than half of all proteins are glycoproteins. Mucintype Oglycosylation is a widespread posttranslational modification of proteins found in the entire animal kingdom, but also in higher plants. The structural complexity of the chains initiated by Olinked GalNAc exceeds that of Nlinked chains by far. The process during which serine and threonine residues of proteins become modified is confined to the cis to trans Golgi compartments. The initiation of this process by peptidyl GalNActransferases is ruled by the sequence context of putative Oglycosylation sites, but also by epigenetic regulatory mechanisms, which can be mediated by enzyme competition. The cellular repertoir of glycosyltransferases with their distinct donor sugar and acceptor sugar specificities, their sequential action at highlyordered surfaces, and their localizations in subcompartments of the Golgi finally determine the cellspecific Oglycosylation profile. Dramatic alterations of the glycosylation machinery are observed in cancer cells, resulting in aberrantly Oglycosylated proteins that expose previously masked peptide motifs and new antigenic targets. The functional aspects of Olinked glycans, which comprise among many others their potential role in sorting and secretion of glycoproteins, their influence on protein conformation, and their multifarious involvement in cell adhesion and immunological processes, appear as complex as their structures.

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Published Online: 2005-06-01
Published in Print: 2001-02-12

Copyright © 2001 by Walter de Gruyter GmbH & Co. KG

Articles in the same Issue

  1. Highlight: Glycobiology
  2. O-Glycosylation of the Mucin Type
  3. Glycoproteins from Insect Cells: Sialylated or Not?
  4. Congenital Disorders of Glycosylation: Glycosylation Defects in Man and Biological Models for Their Study
  5. Mitochondrial Single-Stranded DNA-Binding Proteins: in Search for New Functions
  6. Do Rodent and Human Brains Have Different N-Glycosylation Patterns?
  7. The Liver Flukes Fasciola gigantica and Fasciola hepatica Express the Leucocyte Cluster of Differentiation Marker CD77 (Globotriaosylceramide) in Their Tegument
  8. Cloning and Expression of Drosophila melanogaster UDP-GlcNAc:?-3-D-Mannoside ? 1,2-N-Acetylglucosaminyltransferase I
  9. Pathways of Mucin O-Glycosylation in Normal and Malignant Rat Colonic Epithelial Cells Reveal a Mechanism for Cancer-Associated Sialyl-Tn Antigen Expression
  10. 6-O-Sulfo De-N-Acetylsialyl Lewis X as a Novel High-Affinity Ligand for Human L-Selectin: Total Synthesis and Structural Characterization
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  12. Structural Characterization of Fucose-Containing Oligosaccharides by High-Performance Liquid Chromatography and Matrix-Assisted Laser Desorption/ Ionization Time-of-Flight Mass Spectrometry
  13. Anencephaly: Structural Characterization of Gangliosides in Defined Brain Regions
  14. Acidic Glycerol Lipids of Trichomonas vaginalis and Tritrichomonas foetus
  15. Stimulation of Acid Sphingomyelinase Activity by Lysosomal Lipids and Sphingolipid Activator Proteins
  16. Biosynthesis of N-Acetylneuraminic Acid in Cells Lacking UDP-N-Acetylglucosamine 2-Epimerase/ N-Acetylmannosamine Kinase
  17. Synthesis of Nucleotide-Activated Oligosaccharides by ?-Galactosidase from Bacillus circulans
  18. Elucidation of the Role of Functional Amino Acid Residues of the Small Sialidase from Clostridium perfringens by Site-Directed Mutagenesis
  19. Biosynthesis of Lipid-Linked Oligosaccharides in Yeast: the ALG3 Gene Encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol Mannosyltransferase
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