6533b7ddfe1ef96bd1275294
RESEARCH PRODUCT
The role of the Thomsen-Friedenreich antigen as a tumor-associated molecule.
K H Meyer Zum BüschenfeldeWolfgang DippoldA Steinbornsubject
medicine.drug_classHealth Toxicology and MutagenesisDisaccharidesMonoclonal antibodyMalignancyAntibodiesEpitopeAntigenAntibody SpecificityAntigens NeoplasmTumor Cells CulturedmedicineHumansAntigens Tumor-Associated Carbohydratechemistry.chemical_classificationMolecular StructurebiologyThomsen-Friedenreich AntigenPublic Health Environmental and Occupational Healthmedicine.diseaseMolecular biologyMolecular Weightcarbohydrates (lipids)chemistrybiology.proteinImmunohistochemistryAntibodyCarrier ProteinsGlycoproteinResearch Articledescription
The Thomsen-Friedenreich antigen (Gal-GalNAc) represents a tumor-associated molecule, which is assumed to be one of the few chemically well-defined antigens with a proven association with malignancy. In order to analyze the role of the carbohydrate structure Gal-GalNAc for gastrointestinal tumors, we immunized Balb/c mice with MCF-7 breast tumor cells together with synthetic Gal-GalNAc linked to a BSA carrier. One monoclonal antibody (82-A6) was established which recognizes the Thomsen-Friedenreich antigen according to the biochemical and serological analysis presented here. In contrast to the studies performed in the past, immunohistochemical results using this antibody 82-A6 did not exhibit a reactivity clearly restricted to tumors. Preliminary biochemical analysis revealed that the T-determinant is detectable in the high-molecular weight range (about 1000 kD), suggesting that the Gal-GalNAc epitope is found on mucinlike glycoproteins. Tumor restriction of Thomsen-Friedenreich antigen may therefore be determined either by the protein backbone or by the beta-glycosidic linkage of the carbohydrate structure to the protein.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1990-08-01 | Environmental Health Perspectives |