Recognition of Human Recombinant Myelin Associated Glycoprotein by Anti-carbohydrate Antibodies of the L2/HNK-1 Family

• Published in: Biochemical and biophysical research communications 1995-12, Vol.217 (1), p.171-178
• Main Authors: Bigliardiqi, M., Miescher, G.C., Steck, A.J.
• Format: Article
• Language: English
• Subjects: Antibodies, Monoclonal; Carbohydrates - chemistry; Carbohydrates - immunology; Epitopes - chemistry; Humans; Hybridomas - immunology; Melanoma - immunology; Myelin-Associated Glycoprotein - genetics; Myelin-Associated Glycoprotein - immunology; Recombinant Proteins - genetics; Recombinant Proteins - immunology; Transfection; Tumor Cells, Cultured
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1995.2760

The L2 and HNK-1 monoclonal antibodies recognize carbohydrate determinants containing sulfate-3-glucuronate that are prominent on cells of neural crest lineages. In humans these epitopes are most abundant on the Myelin Associated Glycoprotein and it was assumed that they co-localize on the same molecules. Recently, in vitro synthesized carbohydrates have provided a basis for the different recognition requirements of these two antibodies. We now provide in vivo evidence that a human melanoma cell line can produce glycoproteins such as fibronectin, which is recognized by both the L2 and HNK-1 antibodies, and simultaneously a transfected Myelin Associated Glycoprotein carrying only L2-type carbohydrates. Conceivably, the differential expression of L2-and HNK-1 type glycans could have a role in development.