galactocerebroside and Neuroblastoma

Anti-galactocerebroside (GalC) antibodies have been reported to inhibit myelin formation, cause demyelination, and block HIV-I infection of neural cells. We examined the binding of 3 monoclonal and polyclonal anti-GalC antibodies to a panel of purified glycolipids by ELISA and by an immunospot assay on nitrocellulose blots. All 3 antibodies bound strongly to GM1 ganglioside, monogalactosyl diglyceride, and asialo-GM1, and 2 of the antibodies bound to GD1b and psychosine. The anti-GalC antibodies also bound to 3 glycoprotein bands in human neuroblastoma cells on Western blot, and binding to the proteins was abolished by pre-treatment with pronase or with periodate which oxidizes the terminal carbohydrate residues. These results indicate that anti-GalC antibodies cross react with oligosaccharide determinants of other glycolipids and glycoproteins, and that these cross-reactivities may be responsible for some of the biological effects of the anti-GalC antibodies.

Topics: Animals; Antibody Specificity; Antigens, Neoplasm; Autoantibodies; Carbohydrate Sequence; Cross Reactions; Enzyme-Linked Immunosorbent Assay; Epitopes; Galactosylceramides; Glycolipids; Glycoproteins; Humans; Immunoglobulin M; Mice; Molecular Sequence Data; Motor Neuron Disease; Neoplasm Proteins; Neuroblastoma; Rabbits; Sensation Disorders; Tumor Cells, Cultured