The Journal of Immunology · 1967 · 180 citations · 0 references
Life SciencesImmunologyOncologyCancer ImmunologyGlycobiologyTumor ImmunologyCancer GlycobiologyCell-surface GlycansGlycan RecognitionGlycan StructureTumor AntigensTumor-associated AntigensAdenocarcinoma PathologyCarbohydrate Tumor AntigensGlycolipid AntigensGlycolipid BiosynthesisGlycolipid StructureHydrolysisTumor-associated Carbohydrate AntigensTumor-associated Glycoproteins
Summary A fucose-containing glycolipid isolated from human adenocarcinoma tissue was found to lack blood group A or B activity regardless of the blood type of the tissue donor. The tumor glycolipid had weak H and moderate Lea activity. Tumor glycolipid was precipitated by type XIV pneumococcal polysaccharide antiserum only after mild acid hydrolysis. Antisera to tumor glycolipid agglutinated erythrocytes of type A more strongly than erythrocyte of type B, AB, or O. Furthermore, tumor glycolipid and type A glycolipid inhibited the agglutination of tumor cells by a certain phytoagglutinin more strongly than other glycolipids tested. Thus blood group A substance or erythrocytes appear to contain increased amounts of a hapten structure similar to or identical with the carbohydrate moiety of tumor glycolipid. It is suggested that tumor glycolipid results from an aberration in synthesis of glycolipids possessing blood group activity.