Enzymatic basis of sugar structures of α-fetoprotein in hepatoma and hepatoblastoma cell lines: Correlation with activities of α1–6 fucosyltransferase and N-acetylglucosaminyltransferases III and V
✍ Scribed by Masao Ohno; Atsushi Nishikawa; Masatoshi Koketsu; Hiroko Taga; Yasuo Endo; Toshikazu Hada; Kazuya Higashino; Naoyuki Taniguchi
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- French
- Weight
- 353 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0020-7136
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✦ Synopsis
a-Fetoproteins (AFPs) were purified from 2 hepatoma cell lines (Hep G2 and HUH-7) and a hepatoblastoma cell line (HUH-6), and the structures of pyridylaminated (PA) derivatives of their sugar chains were analyzed by HPLC. Simultaneously, the activities of al-6 fucosyltransferase (a1 -6FT) and N-acetylglucosaminyltransferase 111 (GnT-Ill), IV (GnT-IV) and V (GnT-V) were assayed in these cell lines. For all 3 cell lines the major sugar chain detected was a fucosylated biantennary structure. Hep G2 cells contained a high level of GnT-V, which catalyzes the formation of a tri'-antennary structure, and in fact a substantial percentage of the AFP sugar chains in these cells had the tri'-antennary structure. al-6FT was also high, and fucosylated tri' structures were detected, which suggests that high activities of transferases affect the AFP sugar chains. In HUH-6 cells, GnT-Ill, which catalyzes the formation of bisecting GlcNAc, was elevated. Correspondingly, a fucosylated, bisected biantennary structure was found as a major sugar chain. In the HUH-7 cell line, the contents of bisecting GlcNAc and tri' structure were low and neither GnT-Ill nor GnT-V was elevated. These data indicate that the sugar structures of AFP in these cell lines correlate well with the activities of al-6 FT, GnT-Ill and GnT-V.