N-linked oligosaccharides are not required for neuron-neuron interactions mediated by neural cell adhesion molecule.
Recent studies have described the role of various regions of the neural cell adhesion molecule (NCAM) in cell-cell interactions. Monoclonal antibodies (L2/HNK-1) directed against a sulfated, glucuronic acid-containing, N-linked carbohydrate epitope have also been shown to inhibit NCAM-mediated neural cell adhesion. In the present study we show that dissociated retinal neurons in an in vitro model system can bind as well to normal NCAM as to NCAM lacking the L2/HNK-1 epitope or to glycopeptidase F-treated NCAM. These data suggest that N-linked oligosaccharide chains do not confer upon NCAM the adhesional properties associated with its role in neuron-neuron interactions.
Cole
G J
GJ
Department of Anatomy and Cell Biology, Medical University of South Carolina, Charleston 29425.
Schachner
M
M
Fliesler
S J
SJ
D000581:Amidohydrolases / Q000494:pharmacology; D000818:Animals; D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000502:physiology*; D002448:Cell Adhesion / Q000187:drug effects; D015815:Cell Adhesion Molecules; D002450:Cell Communication; D002642:Chick Embryo; D051379:Mice; D009474:Neurons / Q000502:physiology*; D009844:Oligosaccharides / Q000502:physiology*; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D013433:Sulfoglycosphingolipids / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D015815:Cell Adhesion Molecules; D009844:Oligosaccharides; D013433:Sulfoglycosphingolipids; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase