Morris Hepatomas pp 405-437 | Cite as
Terminal Sugars in Glycoconjugates: Metabolism of Free and Protein-Bound L-Fucose, N-Acetylneuraminic Acid and D-Galactose in Liver and Morris Hepatomas
Summary
1. In Morris hepatomas the activity of UDP-N-acetyl-glucosamine 2′-epimerase, the key enzyme for the synthesis of N-acetylneuraminic acid, was always decreased to about 10%. 2. In all tumors investigated the activity of ADP-galactose 4-epimerase was raised between 2 to 28-fold, whereas the level of galactose 1-phosphate uridyltransferase was lowered. 3. The specific activity of GDP-fucose: glycoprotein fucosyltransferase was elevated between 2 to 3-fold; conversely, the activity of sialyltransferase was generally decreased. 4. In fast growing tumors the content of GDP-fucose was raised between 2 to 3-fold, the concentration of CMP-N-acetylneuraminic acid was more or less unchanged and the content of UDP-galactose markedly decreased. 5. Measurement of the protein-bound carbohydrate content of plasma membranes revealed that none of the neutral sugars showed a significant difference, except for L-fucose, which was greatly increased from 6.1 ± 1.7 nmoles/mg of protein in host or normal liver to 26.1 ± 2.7 nmoles/mg of protein in hepatoma 7777. 6. The specific activity of α-L-fucosidase in hepatomas with a short or intermediate growth rate was 2 to 7-fold higher than in normal liver, the level of neuraminidase and galactosidase lowered or at least remained unchanged. 7. A fucoprotein with a molecular weight of about 130,000 has been isolated from both liver and hepatoma plasma membranes.
The results indicate that specific alterations of free and protein-bound sugars are a characteristic feature of Morris hepatomas.
Keywords
Sugar Nucleotide Host Liver Neuraminic Acid Terminal Sugar Morris HepatomaPreview
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