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Two Monoclonal Antibodies Recognizing Carbohydrate Epitopes on Neural Adhesion Molecules Interfere with Cell Interactions
Author(s) -
Fahrig Thomas,
Schmitz Brigitte,
Weber Dieter,
KüchererEhret Andrea,
Faissner Andreas,
Schachner Melitta
Publication year - 1990
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.1990.tb00407.x
Subject(s) - epitope , monoclonal antibody , neural cell adhesion molecule , glycoprotein , glycan , neurite , antibody , cell adhesion , cell adhesion molecule , biology , chemistry , microbiology and biotechnology , in vitro , biochemistry , cell , immunology
We have studied two monoclonal antibodies raised against crude fractions of membrane glycoproteins from adult mouse brain and found them to react with two carbohydrate epitopes expressed on several neural cell adhesion molecules. Other identified and unidentified glycoproteins from different cell types, organs and species were also recognized by these antibodies. Both epitopes are N‐glycosidically linked mannosidic or hybrid type oligosaccharides and co‐expressed on all the glycoproteins so far tested. In spite of their remarkable similarities, the glycan epitopes are different as shown by ELISA competition assays. In microexplant outgrowth and cell adhesion assays, both antibodies interfere with neural cell adhesion, migration, and neurite outgrowth. These observations, together with previous studies on the L2/HNK‐1 glycan (Künemund et al., 1988), indicate that adhesion molecules carry various carbohydrate epitopes mediating different cell interactions in in vitro assays.