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Modification of Cell Surface Carbohydrates and Invasive Behavior by an Alkyl Lysophospholipid¹

Division of Cell Biology, The Netherlands Cancer Institute, Antoni van Leeuwenhoek Huis, 121 Plesmanlaan, 1066 CX Amsterdam, The Netherlands [J. G. M. B., D. C. C. S., H. v. R., L. A. S.] and Oncologic Centre, Department of Radiotherapy, Academic Hospital Free University, Brussels, Laarbeeklaan 101, 1090 Brussels, Belgium [G. A. S.]

The effect of the alkyl lysophospholipid racemic-1-O-octadecyl-2-O-methyl glycero-3-phosphocholine on the expression of cell surface carbohydrates of four matched pairs of normal and malignant cells was studied using chromatographic techniques. After treatment with alkyl lysophospholipid, glycopeptides proteolytically derived from normal and malignant cells displayed a shift in the size distribution profiles obtained by gel filtration. These drug-induced changes in molecular weight distribution were expressed most strongly in untransformed cells and resembled the carbohydrate alterations found after their malignant transformation. Desialylation abolished the effect of alkyl lysophospholipid, thus suggesting an increased amount of sialic acid in the surface carbohydrates of drug-treated cells.

Chromatography of glycopeptides on concanavalin A-Sepharose, Ricinus communis agglutinin I-agarose, and Bio-Gel P-4 columns excluded a higher degree of branching but suggested addition of extra terminal sialic acid residues as the major cause of the observed alterations. Alkyl lysophospholipid stimulated glycoprotein sialylation of normal cells to the level observed in malignant cells, thus inducing a "malignant-like" surface phenotype. The drug-induced carbohydrate changes in normal chick heart tissue prevented its being invaded by tumor cells when tested in an organotypic assay. The alkyl lysophospholipid thus appears to modulate in a nontoxic fashion the expression of surface molecules implicated in various cellular interactions including invasiveness.

¹ Supported by grants from the Netherlands Cancer Foundation, Koningin Wilhelmina Fonds (NKI-KWF 84-16), Amsterdam, the Netherlands, and from NAVO and Belgisch Werk tegen Kanker, Brussels, Belgium.

² To whom requests for reprints should be addressed.

³ Present address: Bristol-Meyers Belgium, 185–187 Terhulpsesteenweg, 1170 Brussels, Belgium.

Received 10/20/86. Revised 10/13/87. Accepted 11/18/87.