Abstract
The monoclonal L3 antibody reacts with an N-glycosidically linked carbohydrate structure on at least nine glycoproteins of adult mouse brain. Three out of the L3 epitope-carrying glycoproteins could be identified as the neural cell adhesion molecules L1 and myelin-associated glycoprotein, and the novel adhesion molecule on glia. Expression of the L3 carbohydrate epitope is regulated independently of the protein backbone of these three glycoproteins. Based on the observation that out of three functionally characterized L3 epitope-carrying glycoproteins three fulfill the operational definition of an adhesion molecule, we would like to suggest that they form a new family of adhesion molecules that is distinct from the L2/HNK-1 carbohydrate epitope family of neural cell adhesion molecules. Interestingly, some members in each family appear to be unique to one family while other members belong to the two families.
MeSH Terms
Adenosine Triphosphatases
Animals
Antigens, Surface/analysis,immunology
Astrocytes/chemistry
Brain Chemistry
Carbohydrates/immunology
Cation Transport Proteins
Cell Adhesion Molecules
Cell Adhesion Molecules, Neuronal
Cerebellum/chemistry
Epitopes/immunology
Extracellular Matrix Proteins
Fibroblasts/chemistry
Mice
Mice, Inbred Strains
Mice, Nude
Myelin Proteins/immunology
Myelin-Associated Glycoprotein
Neurons/chemistry
Chemicals
Antigens, Surface
Atp1b2 protein, mouse
Carbohydrates
Cation Transport Proteins
Cell Adhesion Molecules
Cell Adhesion Molecules, Neuronal
Epitopes
Extracellular Matrix Proteins
Myelin Proteins
Myelin-Associated Glycoprotein
Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kücherer A
Faissner A
Schachner M
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