Glycolipid antigen expression in human lung cancer.

Several mouse monoclonal antibodies which recognize carbohydrate sequences distinguish between different types of human lung cancer immunohistologically. These antibodies bind to glycolipid antigens produced by the cancer cells. When these glycolipids are separated by thin-layer chromatography, immunostaining of the chromatograms yields complex patterns of antigen-positive bands. To determine whether glycolipid patterns are useful in the classification of lung cancer, 16 human lung cancer cell lines comprising the major histological types of primary lung cancer were studied. Neutral glycolipids and gangliosides were isolated and separated by thin-layer chromatography. Six anti-carbohydrate antibodies which recognize structurally related antigens were used for immunostaining. Neuraminidase treatment of the chromatograms was used to detect "cryptic" sialylated antigens. All the cell lines were unique with regard to the type, amount, and chromatography pattern of the glycolipid antigens produced. Small cell lung cancer cell lines synthesized the greatest variety of antigens, whereas cell lines with large cell cytology synthesized the least. Interestingly, there was an inverse relationship between expression of some glycolipid antigens and DNA amplification of the c-myc oncogene. This suggests that enhanced c-myc expression may influence the types of glycolipids expressed at the surface of lung tumor cells.