Studies on cell adhesion and recognition. I. Extent and specificity of cell adhesion triggered by carbohydrate-reactive proteins (glycosidases and lectins) and by fibronectin.

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Abstract
The extent and the specificity of the initial cell attachment induced by various proteins coated on plastic surfaces have been studied with the following results. Cell adhesion [mouse embryo fibroblast BALB/c 3T3 cells and hamster embryo fibroblast NIL cell] on the surfaces coated with sialidase and .beta.-galactosidase was as strong as on concanavalin A and Limulus lectin-coated surfaces and the reactions were strongly inhibited by glycosidase inhibitors or by competitive substrates. The adhesion on sialidase was inhibited by 2-deoxy-2,3,-dehydro-N-acetylneuraminic acid and by polysialoganglioside (GT1b) at low concentration (0.05-0.1 mM). The cell adhesion on .beta.-galactosidase coat was inhibited by 1,4-D-galactonolactone and .beta.-methylgalactoside but not by .alpha.-methylgalactoside. The initiation of cell adhesion on glycosidase surfaces could be mediated through the interactions of the specific binding sites of the enzyme surface with the cell surface substrates under physiological conditions. Cell adhesion on various lectins could be blocked by various competing monosaccharides at the concentrations similar to the inhibitory concentrations for binding of lectins from solution to the cells. Cell adhesion on fibronectin surfaces as well as on gelatincoated surfaces was equally inhibited by GT1b at relatively high concentrations (0.25-0.5 mM). Lower concentrations of GT1b (0.05-0.1 mM) inhibited the cell adhesion on surfaces of Limulus lectin and sialidase. Apparently, the cell adhesion mediated by fibronectin is based on yet unknown interactions in contrast to a specific cell adhesion through glycosidases and lectins.