Regulation of Glycoprotein Synthesis during Development of the Sea Urchin Embryo

  • William J. Lennarz
Part of the Developmental Biology book series (DEBO, volume 3)


In recent years there has been much progress in our understanding of the assembly mechanism for the oligosaccharide chain of N-linked glycoproteins (Struck and Lennarz, 1980). N-linked glycoproteins fall into two classes—one in which the chains terminate with polymannose residues and a second in which the chains terminate with the trisaccharide consisting of sialic acid, galactose, and N-acetylglucosamine (see Fig. 1). Despite the structural dif ferences in these two types of chains, both have the common feature of an Nglycosidic bond between the innermost N-acetylglucosamine unit and the amino side chain of an asparagine residue in the polypeptide chain. Furthermore, both types of chain are formed via a common precursor, an oligosaccharide that is preassembled in the rough endoplasmic reticulum.


Sialic Acid Mesodermal Cell Oligosaccharide Chain Label Acetate Glycoprotein Synthesis 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • William J. Lennarz
    • 1
  1. 1.M. D. Anderson Hospital and Tumor Institute, Department of Biochemistry and Molecular BiologyThe University of Texas System Cancer CenterHoustonUSA

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