Terminal Sugars in Glycoconjugates: Metabolism of Free and Protein-Bound L-Fucose, N-Acetylneuraminic Acid and D-Galactose in Liver and Morris Hepatomas

  • W. Reutter
  • C. Bauer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 92)

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 Hepatoma 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • W. Reutter
    • 1
  • C. Bauer
    • 1
  1. 1.Biochemisches Institut, UniversitatFreiburgGermany

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