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A comparison of glycosyltransferase activities and malignant properties in normal and transformed cells derived from BALB/c mice.
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1975
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Glycosyltransferase ActivitiesImmunologyGlycobiologyPathologyCellular PharmacologyCell ProliferationPolysaccharideBalb/c MiceCancer BiologyEnzymatic ModificationTumor BiologyBiosynthesisCancer Cell BiologyCancer ResearchGlycosylationTransformed CellsBiochemistryOncogenic AgentCell LinesCell BiologyMalignant DiseaseNatural SciencesComplex PolysaccharidesNormal CellsCellular BiochemistryMedicineCarbohydrate-protein Interaction
The ability of suspensions of BALB/c cells to catalyze the incorporation of nucleotide sugars into complex polysaccharides has been compared. These cells have previously been characterized for concanavalin A-induced agglutinability, tumorigenicity, and malignancy. All of the cell lines tested catalyze transfer of the sugar moieties of cytosine 5-monophosphate N-acetylneuraminic acid, uridine 5-diphosphate galactose, uridine 5-diphosphate N-acetylgalactosamine, uridine 5-diphosphate N-acetylglucosamine, uridine 5-diphosphate glucose, and guanidine 5-diphosphate monnose into glycoproteins and glycolipids. While some transformed lines exhibit alterations in transferase levels, others cannot be distinguished from normal cells. Normal cells, transformed cells that cause tumors that regress, and transformed cells that cause tumors that kill an immunologically competent host show growth-dependent changes in transferase activities. Determining the ability to catalyze carbohydrate transfer is insufficient for predicting the tumorigenic and malignant properties of a cell line.