Add time:07/28/2019         Source:sciencedirect.com

Monoclonal antibodies A5 and C6 have been reported previously to recognize developmentally regulated determinants involving N-acetyllactosamine [Fenderson B.A., O'Brien D.A., Millette C.F. and Eddy E.M. (1984) Devl Biol. 103, 117–128]. In the present study, the specificity of these antibodies was determined by solid-phase radioimmunoassay and by thin-layer chromatography immunostaining using purified glycolipid standards. Antibody A5 recognized N-acetyllactosamine (type 2 chain; Galβ1 → 4GlcNAcβ1 → 3R ), irrespective of branching status. In contrast, antibody C6 recognized the binary N-acetyllactosamine structure carried on lactoisooctaosylceramide (cas 104042-02-6). Antibody C6 did not react with sialosyl or α-galactosyl derivatives of the isooctaosyl structure, including human G10, G8 and bovine G9. Thus, unlike other anti-I antibodies, C6 provides a specific probe for both branching status and absence of terminal chain modification. Monoclonal antibodies A5, C6 and anti-I(Ma) were used to investigate glycosylation changes associated with oncogenic transformation. In contrast to results with lectins, these antibodies preferentially labeled the major glycoproteins of SV40-transformed human embryonic lung fibroblasts, including GP80, GP180, GP200 and GP250. The results suggest that increased expression of unsubstituted polylactosamine core structure at the cell surface follows SV40-transformation.

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