High alpha-2,6-sialylation of <i>N</i>-acetyllactosamine sequences in <i>ras</i>-transformed rat fibroblasts correlates with high invasive potential

Nadia Le Marer, D. Stéhelin

Glycobiology · 1995 · 55 citations · 0 references

Abstract

Through cloning experiments with the FRras EJ4 cell line, previously described to exhibit a Sambucus nigra agglutinin (SNA)+ phenotype, three clones with a SNA- phenotype were isolated. All the selected SNA+ and SNA- clones expressed the ras oncoprotein and cloned in soft agar with the same efficiency. We were interested in studying the adhesion and invasion properties of the FRras cells presenting a SNA + or - phenotype. They were first compared in their biochemical properties and we found that FRras SNA- were characterized by a low alpha-2,6-sialylation of their cell surface glycoproteins and a low beta-galactoside alpha-2,6 sialytransferase activity. Using in vitro invasion assays, FRras cells exhibiting a low alpha-2,6-sialylation on their surface were found to have a low invasive potential compared to their counterpart SNA+. FRras SNA-clones exhibit a different morphology from that of FRras SNA+ clones. Moreover, homotypic aggregation assays indicated that FRras SNA- were more cohesive with each other and adhesion assays showed that they were more adhesive to fibronectin.