Glycoproteins responsive to the neural-inducing effect of concanavalin A in Cynops presumptive ectoderm

Cell Differ. 1984 Apr;14(1):25-31. doi: 10.1016/0045-6039(84)90005-8.


To examine the possible occurrence of receptors in the ectodermal cell surface which apparently mediates the neural-inducing stimulus, a further experiment by using Con A was done in combination with the enzyme treatments. The presumptive ectoderm explants of Cynops gastrula were first treated with neuraminidase to remove sialic acid. Prior to the Con A treatment, the explants were treated with almond glycopeptidase, which cleaves the asparagine linkage between protein and oligosaccharide in glycoprotein and releases the oligosaccharide moiety intact containing mannose residue from the substrate. No neural induction occurred. When the explants were not treated with almond glycopeptidase, the neural induction frequency was found to be the same as that of the explants treated with only Con A. Biochemical analyses showed that when the fixed ectoderm explants were treated with almond glycopeptidase, several oligosaccharides were released and then fractionated by means of Bio-Gel P-4 filtration. Based on the strict specificity of almond glycopeptidase, these oligosaccharides are unmistakably asparagine-linked oligosaccharides with mannose residues. We discuss the hypothesis of involvement of glycoproteins in the first step of molecular events in the neural induction mechanism.

MeSH terms

  • Amidohydrolases / metabolism
  • Animals
  • Concanavalin A / pharmacology*
  • Ectoderm / drug effects
  • Ectoderm / physiology*
  • Embryo, Nonmammalian / physiology
  • Female
  • Gastrula / physiology*
  • Glycoproteins / physiology*
  • Neurons / physiology*
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  • Plant Lectins
  • Salamandridae / physiology*
  • Seeds / enzymology


  • Glycoproteins
  • Plant Lectins
  • Concanavalin A
  • Amidohydrolases
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase