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

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 mole...

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Bibliographic Details
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
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1995.2760