[Structural change of sugar chains of glycoproteins by cell transformation and its application to the diagnosis of cancer].

Abstract

Comparative study by using hydrazinolysis has revealed that the carbohydrate moieties of gamma-glutamyl transpeptidases purified from rat liver and rat AH-66 hepatoma are quite different. The sugar chains of the liver enzyme were all acidic, while 29% of those of hepatoma enzyme was neutral. Three prominent structural differences were found in the acidic sugar chains of the two enzymes: 1) The liver enzyme has asparagine-linked sugar chains with complete outer chain, NeuAc alpha----Gal beta 1----4GlcNAc, while hepatoma enzyme has sugar chains incomplete in their outer chain moieties; 2) Gal beta 1----4GlcNAc beta 1----4GlcNAc group is found in the sugar chains of liver enzyme but not in those of hepatoma enzyme; 3) More than 40% of the sugar chains of hepatoma enzyme contain bisecting N-acetylglucosamine which is not found in those of liver enzyme.

• Authors: A Kobata, K Yamashita
• Journal: Gan no rinsho. Japan journal of cancer clinics (Gan No Rinsho) Vol. 30 Issue 6 Suppl Pg. 545-51 (May 1984) ISSN: 0021-4949 [Print] Japan
• PMID: 6146730 (Publication Type: English Abstract, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• gamma-Glutamyltransferase

Topics

• Animals
• Cattle
• Clinical Enzyme Tests
• Humans
• Liver (enzymology)
• Liver Neoplasms (diagnosis)
• Neoplasms, Experimental (diagnosis)
• Rats
• gamma-Glutamyltransferase (analysis, blood, isolation & purification)