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Role of Glycosylation in Ligand-Receptor Interactions and Signal Transduction Mechanisms

  • M. R. Sairam
Part of the Biochemical Endocrinology book series (BIOEND)

Abstract

Glycosylation of secreted as well as membrane bound proteins in eukaryotic systems represents the most widely occurring covalent and post-translational modification during their biosynthesis. Their wide spectrum of biological activities viz, as membrane receptors, lectins, enzymes, carriers, structural components, hormones, growth stimulatory/ inhibitory factors, accounts for their ubiquitous nature. Although many glycoproteins contain both N-linked as well as O-linked oligosaccharides, the major pathways and the numerous enzymes involved only in the biosynthesis of asparagine linked sugars have been extensively investigated (Schachter et al., 1983; Kornfeld and Kornfeld, 1985). For N-glycosylation the presence of a consensus sequence in the protein Asn-X-Ser (Thr), where X can be any amino acid except proline or aspartic acid, is a necessary but not a sufficient condition in itself. Similar recognition sequence(s) for sites of O-glycosylation are not precisely known. The asparagine linked oligosaccharides are synthesized from a common core precursor, with a structure Glc3 Man9 GlcNAc2, which is then transferred as a unit from the lipid carrier dolichol phosphate to the growing nascent polypeptide chain.

Keywords

Sialic Acid Zona Pellucida Carbohydrate Moiety Sugar Chain Glycoprotein Hormone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • M. R. Sairam
    • 1
  1. 1.Reproduction Research LaboratoryClinical Research Institute of MontrealMontrealCanada

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